ID T0IMM6_9SPHN Unreviewed; 383 AA.
AC T0IMM6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=RLDS_17245 {ECO:0000313|EMBL:EQB13065.1};
OS Sphingobium lactosutens DS20.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1331060 {ECO:0000313|EMBL:EQB13065.1, ECO:0000313|Proteomes:UP000015531};
RN [1] {ECO:0000313|EMBL:EQB13065.1, ECO:0000313|Proteomes:UP000015531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS20 {ECO:0000313|EMBL:EQB13065.1,
RC ECO:0000313|Proteomes:UP000015531};
RX PubMed=24051323;
RA Kumar R., Dwivedi V., Negi V., Khurana J.P., Lal R.;
RT "Draft Genome Sequence of Sphingobium lactosutens Strain DS20T, Isolated
RT from a Hexachlorocyclohexane Dumpsite.";
RL Genome Announc. 1:e00753-13(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:EQB13065.1}.
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DR EMBL; ATDP01000098; EQB13065.1; -; Genomic_DNA.
DR RefSeq; WP_021227045.1; NZ_ATDP01000098.1.
DR AlphaFoldDB; T0IMM6; -.
DR PATRIC; fig|1331060.3.peg.3316; -.
DR eggNOG; COG0404; Bacteria.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000015531; 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:EQB13065.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EQB13065.1}.
FT DOMAIN 21..271
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 383 AA; 41522 MW; 8639659F61F29C33 CRC64;
MSGTDDVTHI EEELPLQTLP LDAWHRDKGA RMVGFAGYHM PIQYEGIMAE HGWTREHAGL
FDVSHMGQLT FTGEGVDAAL EHLLPSDIKG LKPFRQRYSM LLDDEGGILD DLMVSRLGDG
AFDGADIYMV VNGATKYDDI GWMIEHLPDE VTMNHMDEQA LLALQGPEAG EALASLIPDT
ADLLFMQSGL FIWRGVSLWI SRSGYTGEDG FEISVPGEDA RLLADALCAL PQVKPIGLGA
RDSLRLEAGL PLYGHDLTPA ISTIAADLGF AIQKRRREEG GFVGHARVMK ELADGPGARR
VGLRIDGRLP AREGARIFAG SVEVGEVTSG GFAPTIGAPI AMGWVSTPYS AIDTALEIDV
RGKRIAAVVA PMPFVPHRYR RKP
//