ID MTNB_SYNP2 Reviewed; 212 AA.
AC B1XPT3;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 02-NOV-2016, entry version 53.
DE RecName: Full=Methylthioribulose-1-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_01677};
DE Short=MTRu-1-P dehydratase {ECO:0000255|HAMAP-Rule:MF_01677};
DE EC=4.2.1.109 {ECO:0000255|HAMAP-Rule:MF_01677};
GN Name=mtnB {ECO:0000255|HAMAP-Rule:MF_01677};
GN OrderedLocusNames=SYNPCC7002_A0554;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C.,
RA Wang J., Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the dehydration of methylthioribulose-1-
CC phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-
CC phosphate (DK-MTP-1-P). {ECO:0000255|HAMAP-Rule:MF_01677}.
CC -!- CATALYTIC ACTIVITY: S-methyl-5-thio-D-ribulose 1-phosphate = 5-
CC (methylthio)-2,3-dioxopentyl phosphate + H(2)O.
CC {ECO:0000255|HAMAP-Rule:MF_01677}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01677};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01677};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via
CC salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose
CC 1-phosphate: step 2/6. {ECO:0000255|HAMAP-Rule:MF_01677}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. MtnB
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01677}.
DR EMBL; CP000951; ACA98561.1; -; Genomic_DNA.
DR ProteinModelPortal; B1XPT3; -.
DR STRING; 32049.SYNPCC7002_A0554; -.
DR EnsemblBacteria; ACA98561; ACA98561; SYNPCC7002_A0554.
DR KEGG; syp:SYNPCC7002_A0554; -.
DR PATRIC; 23815572; VBISynSp37135_0746.
DR eggNOG; ENOG4107QY0; Bacteria.
DR eggNOG; COG0235; LUCA.
DR HOGENOM; HOG000086153; -.
DR KO; K08964; -.
DR OMA; IRGHGLY; -.
DR OrthoDB; POG091H01SP; -.
DR UniPathway; UPA00904; UER00875.
DR Proteomes; UP000001688; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0046570; F:methylthioribulose 1-phosphate dehydratase activity; IEA:UniProtKB-HAMAP.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR GO; GO:0019509; P:L-methionine biosynthetic process from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR GO; GO:0019284; P:L-methionine biosynthetic process from S-adenosylmethionine; IEA:UniProtKB-HAMAP.
DR Gene3D; 3.40.225.10; -; 1.
DR HAMAP; MF_01677; Salvage_MtnB; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR017714; MethylthioRu-1-P_deHdtase_MtnB.
DR PANTHER; PTHR10640; PTHR10640; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
DR TIGRFAMs; TIGR03328; salvage_mtnB; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Complete proteome; Lyase; Metal-binding;
KW Methionine biosynthesis; Reference proteome; Zinc.
FT CHAIN 1 212 Methylthioribulose-1-phosphate
FT dehydratase.
FT /FTId=PRO_0000357109.
FT METAL 98 98 Zinc. {ECO:0000255|HAMAP-Rule:MF_01677}.
FT METAL 100 100 Zinc. {ECO:0000255|HAMAP-Rule:MF_01677}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 10 200 ismart:Aldolase_II [T]
FT MYHIT 1 208 ihamap:Salvage_MtnB [T]
FT MYHIT 11 199 ipfam:Aldolase_II [T]
SQ SEQUENCE 212 AA; 23635 MW; A1F11578DB75AD4A CRC64;
MSLENQTQKE RLCAVIRQLH TQGKSPATST NYSFLDEDQV IFVSRSGVDK SQFQPEDFIA
VDTMGLPLPP DEGIKPSAET LIHCFIYQNF PGITCVLHTH SVAATLLSGI FAAKQAVTFS
GYEVIKGIAG QTTHETAIAL PIFANDQDMK SFCQQLAQRQ EELNNYGFLI AKHGLYAWGE
TMAIAKRHLE VWEFMLECEL EQLKITPPLA AR
//
|
