ID B9E6S0_MACCJ Unreviewed; 372 AA.
AC B9E6S0;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Aminomethyltransferase {ECO:0000256|ARBA:ARBA00012616, ECO:0000256|HAMAP-Rule:MF_00259};
DE EC=2.1.2.10 {ECO:0000256|ARBA:ARBA00012616, ECO:0000256|HAMAP-Rule:MF_00259};
DE AltName: Full=Glycine cleavage system T protein {ECO:0000256|ARBA:ARBA00031395, ECO:0000256|HAMAP-Rule:MF_00259};
GN Name=gcvT1 {ECO:0000313|EMBL:BAH17888.1};
GN Synonyms=gcvT {ECO:0000256|HAMAP-Rule:MF_00259};
GN OrderedLocusNames=MCCL_1181 {ECO:0000313|EMBL:BAH17888.1};
OS Macrococcus caseolyticus (strain JCSC5402).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX NCBI_TaxID=458233 {ECO:0000313|EMBL:BAH17888.1, ECO:0000313|Proteomes:UP000001383};
RN [1] {ECO:0000313|EMBL:BAH17888.1, ECO:0000313|Proteomes:UP000001383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC5402 {ECO:0000313|EMBL:BAH17888.1,
RC ECO:0000313|Proteomes:UP000001383};
RX PubMed=19074389; DOI=10.1128/JB.01058-08;
RA Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.;
RT "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402,
RT reflecting the ancestral genome of the human-pathogenic staphylococci.";
RL J. Bacteriol. 191:1180-1190(2009).
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. {ECO:0000256|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-
CC methylene-5,6,7,8-tetrahydrofolate + N(6)-[(R)-dihydrolipoyl]-L-
CC lysyl-[protein] + NH4(+); Xref=Rhea:RHEA:16945, Rhea:RHEA-COMP:10475,
CC Rhea:RHEA-COMP:10492, ChEBI:CHEBI:15636, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57453, ChEBI:CHEBI:83100, ChEBI:CHEBI:83143; EC=2.1.2.10;
CC Evidence={ECO:0000256|ARBA:ARBA00043710, ECO:0000256|HAMAP-
CC Rule:MF_00259};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|HAMAP-Rule:MF_00259}.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000256|ARBA:ARBA00008609,
CC ECO:0000256|HAMAP-Rule:MF_00259}.
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DR EMBL; AP009484; BAH17888.1; -; Genomic_DNA.
DR AlphaFoldDB; B9E6S0; -.
DR STRING; 458233.MCCL_1181; -.
DR KEGG; mcl:MCCL_1181; -.
DR eggNOG; COG0404; Bacteria.
DR HOGENOM; CLU_007884_10_2_9; -.
DR Proteomes; UP000001383; 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 {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW Rule:MF_00259}; Reference proteome {ECO:0000313|Proteomes:UP000001383};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00259}.
FT DOMAIN 21..267
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 292..371
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 372 AA; 41807 MW; C8307427F5F5C8C3 CRC64;
MLFLFLTIRR NIMSELKRTP LYEKYLEDGA KVIDFSGWAL PVQFSSIKEE HIAVREDIGM
FDVSHMGEII VEGEHALEYL QYVLTNDASK MTDKKAQYTM ICNEDGGVVD DLVVYKLEEN
KYLLVVNAGN TDIDFEWLKS HKKDGVTITN VSSEYGQIAV QGPKTLEKLA PEVKENISEM
KLFEFLKDVE IFGKNVILSQ SGYTGEYGFE IYCKAEDTLS IWEALLNLGI TPCGLGARDT
LRLEAALPLH GQDLSTEITP YEAKMGFSVK LDKGNFIGKS VLETQKLKGV NRKSAGIELL
ERGIARTDYE VFDKEDNKIG YITSGTQSPL TGRSIALALI NTDFTAIDTE VYVQVRKKRI
PAKVVKTPFH KN
//
