ID GCST_CALS4 Reviewed; 374 AA.
AC Q8RCV9;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 115.
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=TTE0296;
OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Caldanaerobacter.
OX NCBI_TaxID=273068;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX PubMed=11997336; DOI=10.1101/gr.219302;
RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA Wang J., Yu J., Yang H.;
RT "A complete sequence of the T. tengcongensis genome.";
RL Genome Res. 12:689-700(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 + N(6)-[(R)-S(8)-
CC aminomethyldihydrolipoyl]-L-lysyl-[protein] = (6R)-5,10-methylene-
CC 5,6,7,8-tetrahydrofolate + N(6)-[(R)-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}.
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DR EMBL; AE008691; AAM23592.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8RCV9; -.
DR SMR; Q8RCV9; -.
DR STRING; 273068.TTE0296; -.
DR KEGG; tte:TTE0296; -.
DR eggNOG; COG0404; Bacteria.
DR HOGENOM; CLU_007884_10_2_9; -.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000000555; 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; 2.40.30.110; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 4.10.1250.10; Aminomethyltransferase fragment; 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 NCBIfam; TIGR00528; gcvT; 1.
DR PANTHER; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR43757:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR PIRSF; PIRSF006487; GcvT; 1.
DR SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR SUPFAM; SSF103025; Folate-binding domain; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Reference proteome; Transferase.
FT CHAIN 1..374
FT /note="Aminomethyltransferase"
FT /id="PRO_0000122613"
SQ SEQUENCE 374 AA; 42167 MW; 9F14391AEDB6B602 CRC64;
MKGCDSLDNL KKTPLYEIYP KYNAKIIDFA GWAMPVQFES IISEHEAVRN AAGLFDVSHM
GEIIVKGKDA FPFLQNLLTN DLSKLNDNQV LYTFMCNHNG GVIDDLLVYK YSNNYYLLVV
NAANIEKDYK WMLNNAGIYK VEIENVSDKI AELAIQGPKA EEILQKLTDE DLSQIKFFYF
KDKVKIAGVE CLVSRTGYTG EDGFEIYMPN EHAVTLWEKI LEAGKDYGLK PAGLGARDTL
RFEAGLPLYG NELGEDITPL EAGLGFFVKF DKGNFIGKDA LLKQKEQGLK RKLVGFEMIG
NGIPRHGYEV QADNQKIGYV TTGYFSPTLK KNIGLALIDS KYAQIGNQIE VIIRNKPLKA
VIVDKNFYKK NYKK
//
