ID   GCST_AQUAE              Reviewed;         350 AA.
AC   O67441;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   23-FEB-2022, entry version 114.
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}; OrderedLocusNames=aq_1458;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. {ECO:0000255|HAMAP-Rule:MF_00259}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-
CC         aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-
CC         5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] +
CC         NH4(+); Xref=Rhea:RHEA:16945, Rhea:RHEA-COMP:10475, Rhea:RHEA-
CC         COMP:10492, ChEBI:CHEBI:15636, ChEBI:CHEBI:28938, ChEBI:CHEBI:57453,
CC         ChEBI:CHEBI:83100, ChEBI:CHEBI:83143; EC=2.1.2.10;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00259};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. {ECO:0000255|HAMAP-Rule:MF_00259}.
CC   -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000255|HAMAP-
CC       Rule:MF_00259}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC07401.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AE000657; AAC07401.1; ALT_FRAME; Genomic_DNA.
DR   PIR; G70426; G70426.
DR   STRING; 224324.aq_1458; -.
DR   EnsemblBacteria; AAC07401; AAC07401; aq_1458.
DR   eggNOG; COG0404; Bacteria.
DR   HOGENOM; CLU_007884_10_2_0; -.
DR   InParanoid; O67441; -.
DR   OMA; MPVQYPA; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1360.120; -; 1.
DR   HAMAP; MF_00259; GcvT; 1.
DR   InterPro; IPR006223; GCS_T.
DR   InterPro; IPR022903; GCS_T_bac.
DR   InterPro; IPR028896; GCST/YgfZ/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; PTHR43757; PTHR43757; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   SUPFAM; SSF101790; SSF101790; 1.
DR   TIGRFAMs; TIGR00528; gcvT; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Reference proteome; Transferase.
FT   CHAIN           1..350
FT                   /note="Aminomethyltransferase"
FT                   /id="PRO_0000122534"
SQ   SEQUENCE   350 AA;  40336 MW;  688BFC891407A0FB CRC64;
     MILFYFMQTP LYYVHKHLKA KFTNFAGWTM PLQYTSIIEE VRAVRXRAGV FDISHMGRLL
     IEDPEKKLQY FTTNNLDKLS VGKVQYNLLP NEKGGIKDDV TVYMLSEIEF FLCVNAANRQ
     KVINWLSPHL KLRDLSGELV QIALQGPKSE EIISKFYPVS DLKYYRFKVF DKTIISRTGY
     TGEDGFEIYV SPEEGKELFL ELVKLAKPCG LGARDVLRIE AGLPLYGNEL SEEITPIEVN
     LEKFVDFSKE FIGKEAMLKK KVKKKLFGLE LTEKGIPRKG YRVFKGDREI GWISSGTYSP
     TLNKGIALCF VDIEERKEGN EVEIEVRGRR VRGVLRKYPF VRTPAGRYQK