ID T0K527_9SPHN Unreviewed; 384 AA.
AC T0K527;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=aminomethyltransferase {ECO:0000256|ARBA:ARBA00012616};
DE EC=2.1.2.10 {ECO:0000256|ARBA:ARBA00012616};
DE AltName: Full=Glycine cleavage system T protein {ECO:0000256|ARBA:ARBA00031395};
GN ORFNames=M529_13390 {ECO:0000313|EMBL:EQB31769.1};
OS Sphingobium ummariense RL-3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1346791 {ECO:0000313|EMBL:EQB31769.1, ECO:0000313|Proteomes:UP000015523};
RN [1] {ECO:0000313|EMBL:EQB31769.1, ECO:0000313|Proteomes:UP000015523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RL-3 {ECO:0000313|EMBL:EQB31769.1,
RC ECO:0000313|Proteomes:UP000015523};
RX PubMed=24233594;
RA Kohli P., Dua A., Sangwan N., Oldach P., Khurana J.P., Lal R.;
RT "Draft Genome Sequence of Sphingobium ummariense Strain RL-3, a
RT Hexachlorocyclohexane-Degrading Bacterium.";
RL Genome Announc. 1:e00956-13(2013).
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};
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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:EQB31769.1}.
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DR EMBL; AUWY01000091; EQB31769.1; -; Genomic_DNA.
DR RefSeq; WP_021318469.1; NZ_AUWY01000091.1.
DR AlphaFoldDB; T0K527; -.
DR STRING; 1346791.M529_13390; -.
DR PATRIC; fig|1346791.3.peg.2576; -.
DR eggNOG; COG0404; Bacteria.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000015523; Unassembled WGS sequence.
DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
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 InterPro; IPR006223; GCS_T.
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};
KW Methyltransferase {ECO:0000313|EMBL:EQB31769.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015523};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EQB31769.1}.
FT DOMAIN 21..270
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 299..375
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 384 AA; 41306 MW; 8DCAD24DFDB6AD98 CRC64;
MTGKDDVATL EEELPLVELP LDAWHRAKGA RMVGFAGYHM PIQYEGIMAE HAWTREHAGL
FDVSHMGQLG FSGEGVDEAL EVLLPSDIKG LKPFRQRYSM LLDEEGGILD DLMVSRLGDG
AFDGAEIYMV VNGATKYDDI GWMIEHLPDE VVMNHMDEQA LLALQGPEAG DAMAALVPGT
AELLFMQSGL FTWRGVPLWI SRSGYTGEDG FEISVPADSV QLLADALCAL PQVKPVGLGA
RDSLRLEAGL PLYGHDLDSR VSTIGADLGF AIQKRRREEG GFIGHARVLK ELADGPGTKR
VGLTIEGRLP AREGAQIYSG ANLVGEVTSG GFAPTVGAPI AMGWVSLPHA ALGTALEIEV
RGKRIGATVA PMPFVPHRYR RAKS
//
