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=Aminomethyltransferase {ECO:0000255|HAMAP-Rule:MF_00259}; EC=2.1.2.10 {ECO:0000255|HAMAP-Rule:MF_00259}; AltName: Full=Glycine cleavage system T protein {ECO:0000255|HAMAP-Rule:MF_00259}; |
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| MyHits synonyms | GCST_BURMA , Q62FM9 , 0EE9681AF1660350 |
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ID GCST_BURMA Reviewed; 372 AA.
AC Q62FM9;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 05-OCT-2016, entry version 72.
DE RecName: Full=Aminomethyltransferase {ECO:0000255|HAMAP-Rule:MF_00259};
DE EC=2.1.2.10 {ECO:0000255|HAMAP-Rule:MF_00259};
DE AltName: Full=Glycine cleavage system T protein {ECO:0000255|HAMAP-Rule:MF_00259};
GN Name=gcvT {ECO:0000255|HAMAP-Rule:MF_00259};
GN OrderedLocusNames=BMA2994.1;
OS Burkholderia mallei (strain ATCC 23344).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=243160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23344;
RX PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M.,
RA Daugherty S.C., Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F.,
RA Madupu R., Mohammoud Y., Nelson W.C., Radune D., Romero C.M.,
RA Sarria S., Selengut J., Shamblin C., Sullivan S.A., White O., Yu Y.,
RA Zafar N., Zhou L., Fraser C.M.;
RT "Structural flexibility in the Burkholderia mallei genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. {ECO:0000255|HAMAP-Rule:MF_00259}.
CC -!- CATALYTIC ACTIVITY: [Protein]-S(8)-aminomethyldihydrolipoyllysine
CC + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-
CC methylenetetrahydrofolate + NH(3). {ECO:0000255|HAMAP-
CC Rule:MF_00259}.
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins:
CC P, T, L and H. {ECO:0000255|HAMAP-Rule:MF_00259}.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000255|HAMAP-
CC Rule:MF_00259}.
DR EMBL; CP000010; AAU50158.1; -; Genomic_DNA.
DR RefSeq; WP_004202927.1; NC_006348.1.
DR RefSeq; YP_104498.1; NC_006348.1.
DR ProteinModelPortal; Q62FM9; -.
DR STRING; 243160.BMA2994.1; -.
DR EnsemblBacteria; AAU50158; AAU50158; BMA2994.1.
DR GeneID; 3089933; -.
DR KEGG; bma:BMA2994.1; -.
DR PATRIC; 19121159; VBIBurMal55007_3072.
DR eggNOG; ENOG4105D43; Bacteria.
DR eggNOG; COG0404; LUCA.
DR HOGENOM; HOG000239381; -.
DR KO; K00605; -.
DR OMA; HSPILNM; -.
DR Proteomes; UP000006693; Chromosome 1.
DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-HAMAP.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-HAMAP.
DR Gene3D; 2.40.30.110; -; 1.
DR Gene3D; 3.30.1360.120; -; 2.
DR HAMAP; MF_00259; GcvT; 1.
DR InterPro; IPR006223; GCS_T.
DR InterPro; IPR022903; GCS_T_bac.
DR InterPro; IPR028896; GCST/DmdA.
DR InterPro; IPR013977; GCV_T_C.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR029043; GcvT/YgfZ_C.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR PANTHER; PTHR13847:SF5; PTHR13847:SF5; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR PIRSF; PIRSF006487; GcvT; 1.
DR SUPFAM; SSF101790; SSF101790; 1.
DR TIGRFAMs; TIGR00528; gcvT; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Complete proteome; Transferase.
FT CHAIN 1 372 Aminomethyltransferase.
FT /FTId=PRO_0000122549.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 3 366 ihamap:GcvT [T]
FT MYHIT 270 361 ipfam:GCV_T_C [T]
FT MYHIT 9 262 ipfam:GCV_T [T]
SQ SEQUENCE 372 AA; 40093 MW; 0EE9681AF1660350 CRC64;
MTVLKTTPLH AAHRALNARM VDFGGWDMPV NYGSQIEEHQ AVRTDAGMFD VSHMCVVDFT
GPRVRAFFEH AIANNVAKLQ TPGKALYSCL LNPQGGVIDD LIVYYFTEEF FRVVVNAGTA
EKDIAWFNQL NEQGGFGLTI APRRDFAIVA AQGPNARAKV WDTVPCARAA TSELKPFNAA
QVAGTPFGDL TVARTGYTGE DGFEIIVPAT HVEALWNALA ERGVRPCGLG ARDTLRLEAG
MNLYGQDMDE SVSPLDAGLA WTVDLSAPRA FVGRDALEAH GSRAAFVGLI LQKENGRAGG
VLRAHQKVAT PHGEGEITSG TFSPSMQESI AFARVPKDVA IGDTVHVQIR DKQLPARVVK
LPFVRNGKVL AA
//
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