ID   GCST_OCEIH              Reviewed;         371 AA.
AC   Q8CXD9;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2003, sequence version 2.
DT   25-MAY-2022, entry version 106.
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=OB1904;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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=BAC13860.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000028; BAC13860.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q8CXD9; -.
DR   SMR; Q8CXD9; -.
DR   STRING; 221109.22777588; -.
DR   EnsemblBacteria; BAC13860; BAC13860; BAC13860.
DR   KEGG; oih:OB1904; -.
DR   eggNOG; COG0404; Bacteria.
DR   HOGENOM; CLU_007884_10_2_9; -.
DR   PhylomeDB; Q8CXD9; -.
DR   Proteomes; UP000000822; Chromosome.
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..371
FT                   /note="Aminomethyltransferase"
FT                   /id="PRO_0000122579"
SQ   SEQUENCE   371 AA;  41336 MW;  EA04379D38752217 CRC64;
     MSEQKRTPIF TEYASHGAKT IDFGGWDLPV QFSSIKHEHE VTRTKAGLFD VSHMGEISVK
     GPKSESFLQY VLTNDISKLE PGKAQYTIMC YEDGGTVDDL IVYKLDDEDY LLVVNAANTE
     KDANWIKQKN TYSNDEIVIE DVSNQYVQLA IQGPKAVEIL QKCTDENVQE IKFFRFKNNV
     ALKGIEAKAL ISRTGYTGED GFEIYIDASS GVALWKLLLE KGEANGLEPI GLGARDTLRF
     EANLALYGQE LSKDISPIEA GLGFAVKVNK GPDFIGKEVL KNQVENGTDR KLVGIEMIDK
     GIPRHEYEVL KDNKEIGFIT SGTQSPTLNK NVGLALINIS YTEIGTEVDV KVRKRILKAK
     IVPTPFYKRG R