MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000303|PubMed:14557261}; Short=GlcNAc 6-P deacetylase {ECO:0000303|PubMed:14557261}; EC=3.5.1.25 {ECO:0000250|UniProtKB:P0AF18}; |
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| MyHits synonyms | NAGA_BACSU , O34450 , 852D53C71BAD6F54 |
 Legends: 1, ACT_SITE Proton donor. {ECO:0000305|PubMed:14557261}; 2, Iron 1; via tele nitrogen. {ECO:0000269|PubMed:14557261}; 3, Iron 1. {ECO:0000269|PubMed:14557261}; 4, Iron 2. {ECO:0000269|PubMed:14557261}; 5, Iron 2; via tele nitrogen. {ECO:0000269|PubMed:14557261}; 6, BINDING Substrate. {ECO:0000250|UniProtKB:P0AF18}; 7, REGION Substrate binding. {ECO:0000269|PubMed:14557261}; 8, STRAND {ECO:0000244|PDB:2VHL}; 9, HELIX {ECO:0000244|PDB:2VHL}; 10, TURN {ECO:0000244|PDB:2VHL}.
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ID NAGA_BACSU Reviewed; 396 AA.
AC O34450;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 02-NOV-2016, entry version 120.
DE RecName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000303|PubMed:14557261};
DE Short=GlcNAc 6-P deacetylase {ECO:0000303|PubMed:14557261};
DE EC=3.5.1.25 {ECO:0000250|UniProtKB:P0AF18};
GN Name=nagA; OrderedLocusNames=BSU35010;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C.,
RA Karamata D.;
RT "Nucleotide sequence of the 300-304 chromosomal segment of Bacillus
RT subtilis.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH IRON AND
RP REACTION PRODUCT, FUNCTION, COFACTOR, SUBUNIT, AND REACTION MECHANISM.
RC STRAIN=168 / IG20;
RX PubMed=14557261; DOI=10.1074/jbc.M310165200;
RA Vincent F., Yates D., Garman E., Davies G.J., Brannigan J.A.;
RT "The three-dimensional structure of the N-acetylglucosamine-6-
RT phosphate deacetylase, NagA, from Bacillus subtilis: a member of the
RT urease superfamily.";
RL J. Biol. Chem. 279:2809-2816(2004).
CC -!- FUNCTION: Involved in the first committed step in the biosynthesis
CC of amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-
CC acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to
CC yield glucosamine 6-phosphate and acetate.
CC {ECO:0000269|PubMed:14557261}.
CC -!- CATALYTIC ACTIVITY: N-acetyl-D-glucosamine 6-phosphate + H(2)O =
CC D-glucosamine 6-phosphate + acetate.
CC {ECO:0000250|UniProtKB:P0AF18}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:14557261};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000269|PubMed:14557261};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation;
CC D-fructose 6-phosphate from N-acetylneuraminate: step 4/5.
CC {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14557261}.
CC -!- SIMILARITY: Belongs to the NagA family. {ECO:0000305}.
DR EMBL; AF017113; AAC67285.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15506.1; -; Genomic_DNA.
DR PIR; A69664; A69664.
DR RefSeq; NP_391381.1; NC_000964.3.
DR RefSeq; WP_003243413.1; NZ_JNCM01000033.1.
DR PDB; 2VHL; X-ray; 2.05 A; A/B=1-396.
DR PDBsum; 2VHL; -.
DR ProteinModelPortal; O34450; -.
DR SMR; O34450; -.
DR STRING; 224308.Bsubs1_010100018951; -.
DR MEROPS; M38.983; -.
DR PaxDb; O34450; -.
DR EnsemblBacteria; CAB15506; CAB15506; BSU35010.
DR GeneID; 936621; -.
DR KEGG; bsu:BSU35010; -.
DR PATRIC; 18979008; VBIBacSub10457_3666.
DR eggNOG; ENOG4105CE4; Bacteria.
DR eggNOG; COG1820; LUCA.
DR HOGENOM; HOG000275009; -.
DR InParanoid; O34450; -.
DR KO; K01443; -.
DR OMA; AFITDAM; -.
DR PhylomeDB; O34450; -.
DR BioCyc; BSUB:BSU35010-MONOMER; -.
DR SABIO-RK; O34450; -.
DR UniPathway; UPA00629; UER00683.
DR EvolutionaryTrace; O34450; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006046; P:N-acetylglucosamine catabolic process; IDA:UniProtKB.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00854; NagA; 1.
DR Gene3D; 2.30.40.10; -; 2.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR003764; GlcNAc_6-P_deAcase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF01979; Amidohydro_1; 1.
DR PIRSF; PIRSF038994; NagA; 1.
DR SUPFAM; SSF51338; SSF51338; 2.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR00221; nagA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Complete proteome; Hydrolase;
KW Iron; Metal-binding; Reference proteome.
FT CHAIN 1 396 N-acetylglucosamine-6-phosphate
FT deacetylase.
FT /FTId=PRO_0000170914.
FT REGION 147 148 Substrate binding.
FT {ECO:0000269|PubMed:14557261}.
FT REGION 226 227 Substrate binding.
FT {ECO:0000269|PubMed:14557261}.
FT REGION 255 258 Substrate binding.
FT {ECO:0000269|PubMed:14557261}.
FT REGION 314 316 Substrate binding.
FT {ECO:0000269|PubMed:14557261}.
FT ACT_SITE 281 281 Proton donor.
FT {ECO:0000305|PubMed:14557261}.
FT METAL 63 63 Iron 1; via tele nitrogen.
FT {ECO:0000269|PubMed:14557261}.
FT METAL 65 65 Iron 1; via tele nitrogen.
FT {ECO:0000269|PubMed:14557261}.
FT METAL 136 136 Iron 1. {ECO:0000269|PubMed:14557261}.
FT METAL 136 136 Iron 2. {ECO:0000269|PubMed:14557261}.
FT METAL 202 202 Iron 2; via tele nitrogen.
FT {ECO:0000269|PubMed:14557261}.
FT METAL 223 223 Iron 2; via tele nitrogen.
FT {ECO:0000269|PubMed:14557261}.
FT METAL 281 281 Iron 1. {ECO:0000269|PubMed:14557261}.
FT BINDING 234 234 Substrate.
FT {ECO:0000250|UniProtKB:P0AF18}.
FT STRAND 5 13 {ECO:0000244|PDB:2VHL}.
FT STRAND 18 27 {ECO:0000244|PDB:2VHL}.
FT STRAND 30 37 {ECO:0000244|PDB:2VHL}.
FT STRAND 44 48 {ECO:0000244|PDB:2VHL}.
FT STRAND 54 57 {ECO:0000244|PDB:2VHL}.
FT STRAND 59 64 {ECO:0000244|PDB:2VHL}.
FT HELIX 72 74 {ECO:0000244|PDB:2VHL}.
FT HELIX 77 86 {ECO:0000244|PDB:2VHL}.
FT HELIX 87 90 {ECO:0000244|PDB:2VHL}.
FT STRAND 92 98 {ECO:0000244|PDB:2VHL}.
FT HELIX 104 120 {ECO:0000244|PDB:2VHL}.
FT HELIX 123 125 {ECO:0000244|PDB:2VHL}.
FT STRAND 126 136 {ECO:0000244|PDB:2VHL}.
FT STRAND 138 140 {ECO:0000244|PDB:2VHL}.
FT HELIX 142 144 {ECO:0000244|PDB:2VHL}.
FT HELIX 150 152 {ECO:0000244|PDB:2VHL}.
FT HELIX 158 167 {ECO:0000244|PDB:2VHL}.
FT TURN 168 170 {ECO:0000244|PDB:2VHL}.
FT STRAND 172 177 {ECO:0000244|PDB:2VHL}.
FT HELIX 179 181 {ECO:0000244|PDB:2VHL}.
FT HELIX 183 185 {ECO:0000244|PDB:2VHL}.
FT HELIX 186 193 {ECO:0000244|PDB:2VHL}.
FT STRAND 197 200 {ECO:0000244|PDB:2VHL}.
FT HELIX 207 215 {ECO:0000244|PDB:2VHL}.
FT STRAND 220 223 {ECO:0000244|PDB:2VHL}.
FT STRAND 226 228 {ECO:0000244|PDB:2VHL}.
FT STRAND 233 235 {ECO:0000244|PDB:2VHL}.
FT HELIX 237 244 {ECO:0000244|PDB:2VHL}.
FT STRAND 249 253 {ECO:0000244|PDB:2VHL}.
FT STRAND 255 259 {ECO:0000244|PDB:2VHL}.
FT HELIX 261 271 {ECO:0000244|PDB:2VHL}.
FT STRAND 275 279 {ECO:0000244|PDB:2VHL}.
FT TURN 284 287 {ECO:0000244|PDB:2VHL}.
FT STRAND 290 295 {ECO:0000244|PDB:2VHL}.
FT STRAND 298 303 {ECO:0000244|PDB:2VHL}.
FT STRAND 306 308 {ECO:0000244|PDB:2VHL}.
FT HELIX 321 332 {ECO:0000244|PDB:2VHL}.
FT HELIX 336 343 {ECO:0000244|PDB:2VHL}.
FT HELIX 345 351 {ECO:0000244|PDB:2VHL}.
FT TURN 354 356 {ECO:0000244|PDB:2VHL}.
FT STRAND 357 359 {ECO:0000244|PDB:2VHL}.
FT STRAND 368 371 {ECO:0000244|PDB:2VHL}.
FT STRAND 377 382 {ECO:0000244|PDB:2VHL}.
FT STRAND 385 389 {ECO:0000244|PDB:2VHL}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 54 386 ipfam:Amidohydro_1 [T]
SQ SEQUENCE 396 AA; 42622 MW; 852D53C71BAD6F54 CRC64;
MAESLLIKDI AIVTENEVIK NGYVGINDGK ISTVSTERPK EPYSKEIQAP ADSVLLPGMI
DIHIHGGYGA DTMDASFSTL DIMSSRLPEE GTTSFLATTI TQEHGNISQA LVNAREWKAA
EESSLLGAEL LGIHLEGPFV SPKRAGAQPK EWIRPSDVEL FKKWQQEAGG LIKIVTLAPE
EDQHFELIRH LKDESIIASM GHTDADSALL SDAAKAGASH MTHLYNAMSP FHHREPGVIG
TALAHDGFVT ELIADGIHSH PLAAKLAFLA KGSSKLILIT DSMRAKGLKD GVYEFGGQSV
TVRGRTALLS DGTLAGSILK MNEGARHMRE FTNCSWTDIA NITSENAAKQ LGIFDRKGSV
TVGKDADLVI VSSDCEVILT ICRGNIAFIS KEADQI
//
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