ID A0A323VCE8_9ACTN Unreviewed; 372 AA.
AC A0A323VCE8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 ECO:0000313|EMBL:PZA22504.1};
GN ORFNames=DMO24_04635 {ECO:0000313|EMBL:PZA22504.1}, FHX36_001450
GN {ECO:0000313|EMBL:MBB3675715.1};
OS Modestobacter versicolor.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=429133 {ECO:0000313|EMBL:PZA22504.1, ECO:0000313|Proteomes:UP000247602};
RN [1] {ECO:0000313|EMBL:PZA22504.1, ECO:0000313|Proteomes:UP000247602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CP153-2 {ECO:0000313|EMBL:PZA22504.1,
RC ECO:0000313|Proteomes:UP000247602};
RA Gundlapally S.R.;
RT "Draft genome sequence of Modestobacter versicolor CP153-2.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB3675715.1, ECO:0000313|Proteomes:UP000580718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16678 {ECO:0000313|EMBL:MBB3675715.1,
RC ECO:0000313|Proteomes:UP000580718};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2020) 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:PZA22504.1}.
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DR EMBL; JACIBU010000001; MBB3675715.1; -; Genomic_DNA.
DR EMBL; QKNV01000029; PZA22504.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A323VCE8; -.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000247602; Unassembled WGS sequence.
DR Proteomes; UP000580718; 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 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:PZA22504.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000247602};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00259}.
FT DOMAIN 8..264
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 288..367
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 372 AA; 38049 MW; 329AE5CFD0A45A53 CRC64;
MSSSTSPLHG RHAAAGAKFA DFGGWSMPIE YAGGGVLAEH TAVREGVGLF DVSHLGTATV
RGPGAADFVN ACLTNDLGRI GPGQAQYTLC CLPDGEDRAG GVVDDLIVYL HGPDDVLLVP
NAANAAAVLA RLAEAAPAGV TVTDRHTEVA VLALQGPRSA EVLAAVGLPG ALGYMSFAGT
PGSGGDEVTV CRTGYTGEHG YELLVGADRA GALWDALLAA GEPEQIRPCG LGARDTLRTE
MGYPLHGHEL SVDITPNQAR SGWAVGWAKD AFWGREALLA ERAAGPARQL WGLQAPGRGI
PRPGMSVLGA DGAVIGEVTS GTFSPTLRTG IALALLDTAA GAGEGTEVAV DVRGRPQPVV
VRRPPFVPSH VR
//
