ID A0A2P8D4Y2_9ACTN Unreviewed; 367 AA.
AC A0A2P8D4Y2;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=gcvT {ECO:0000256|HAMAP-Rule:MF_00259};
GN ORFNames=CLV63_11828 {ECO:0000313|EMBL:PSK92271.1};
OS Murinocardiopsis flavida.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Murinocardiopsis.
OX NCBI_TaxID=645275 {ECO:0000313|EMBL:PSK92271.1, ECO:0000313|Proteomes:UP000240542};
RN [1] {ECO:0000313|EMBL:PSK92271.1, ECO:0000313|Proteomes:UP000240542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45312 {ECO:0000313|EMBL:PSK92271.1,
RC ECO:0000313|Proteomes:UP000240542};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PSK92271.1}.
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DR EMBL; PYGA01000018; PSK92271.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8D4Y2; -.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000240542; Unassembled WGS sequence.
DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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 GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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}; Methyltransferase {ECO:0000313|EMBL:PSK92271.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000240542};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00259}.
FT DOMAIN 10..260
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 286..364
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 367 AA; 38789 MW; B0A247A25A887E94 CRC64;
MPADPRTTPL HEVHKRLGAN LVDFAGWVMP LRYGSETTEH QAVRETAGLF DLSHMGEIHV
AGPQAAEFLD YALVGYLSKV TVGRARYTMI TDADGGVLDD IIVYRLAEDD YLVVANAANS
STVLAALADR VTGFEATVED RSADYALIAV QGPKAVDILA PLTDADLAAI KYYAGYSHTV
AGCAVLLART GYTGEDGFEI FADPGDAARV WEALTESGAA HGLRPAGLSA RDTLRLEAGM
PLYGNELSTD ITPFEAGLGR VVKLEKPGDF VGRAALAARA ESGPRRVLVG LRGRGRRVPR
QGHTVLRDGV PVGTVTSGAP SPTLGAPIAM ASVDAATDLT SGAFAVDVRG RAEDADLVEL
PFYDRNR
//
