ID   GCST_ALCBS              Reviewed;         359 AA.
AC   Q0VLA6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Aminomethyltransferase;
DE            EC=2.1.2.10;
DE   AltName: Full=Glycine cleavage system T protein;
GN   Name=gcvT; OrderedLocusNames=ABO_2594;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine (By similarity).
CC   -!- CATALYTIC ACTIVITY: [Protein]-S(8)-aminomethyldihydrolipoyllysine
CC       + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-
CC       methylenetetrahydrofolate + NH(3).
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins:
CC       P, T, L and H (By similarity).
CC   -!- SIMILARITY: Belongs to the gcvT family.
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DR   EMBL; AM286690; CAL18042.1; -; Genomic_DNA.
DR   RefSeq; YP_694314.1; -.
DR   GeneID; 4211692; -.
DR   GenomeReviews; AM286690_GR; ABO_2594.
DR   KEGG; abo:ABO_2594; -.
DR   NMPDR; fig|393595.12.peg.2598; -.
DR   HOGENOM; Q0VLA6; -.
DR   OMA; Q0VLA6; VEIRGKW.
DR   BioCyc; ABOR393595:ABO_2594-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004047; F:aminomethyltransferase activity; IEA:HAMAP.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavag...; IEA:HAMAP.
DR   HAMAP; MF_00259; -; 1.
DR   InterPro; IPR013977; GCV_T_C.
DR   InterPro; IPR006222; GCV_T_N.
DR   InterPro; IPR006223; GcvT.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   PIRSF; PIRSF006487; GcvT; 1.
DR   TIGRFAMs; TIGR00528; gcvT; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Complete proteome; Transferase.
FT   CHAIN         1    359       Aminomethyltransferase.
FT                                /FTId=PRO_1000047643.
SQ   SEQUENCE   359 AA;  39186 MW;  33D8B0E2D0C7EA74 CRC64;
     MAHRTALYDA HLAAGGKMVD FGGWDMPINY GSQIEEHHAV RQNAGVFDVS HMTVVDIAGA
     GARDYLRQLL ANDVDRIDPG RALYTGMLND NGGVIDDLIV YKRDNDYRLV VNCATRETDL
     GWMEKHAGGF AVDIHERPEL AMLAIQGPKA RDILAGLLNG SRADAVKSLK VFAFAEDGDW
     MIARTGYTGE DGVEIMLPNA DALTLWEQLL EAGVSPIGLG ARDTLRLEAG LNLYGNDMDE
     SITPWEANMG WTVMLNDREF IGRQPLLNQK ENGHSEQVGL ILEGKGVLRA HQKVLMPNGE
     EGEITSGTFS PTLGKSIALA RLPAGATGKV DVEIRNKRQV AQVVKPPFVR NGNAVYKEQ
//