ID A0A0T6UXC0_9PSED Unreviewed; 374 AA.
AC A0A0T6UXC0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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 Name=gcvT {ECO:0000313|EMBL:KRW62624.1};
GN ORFNames=AO726_04190 {ECO:0000313|EMBL:KRW62624.1};
OS Pseudomonas sp. TTU2014-080ASC.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1729724 {ECO:0000313|EMBL:KRW62624.1, ECO:0000313|Proteomes:UP000051864};
RN [1] {ECO:0000313|EMBL:KRW62624.1, ECO:0000313|Proteomes:UP000051864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTU2014-080ASC {ECO:0000313|EMBL:KRW62624.1,
RC ECO:0000313|Proteomes:UP000051864};
RA Webb H.E., Bugarel M., Den Bakker H.C., Nightingale K., Granier S.A.,
RA Loneragan G.H.;
RT "Carbapenem-non-susceptible Bacteria Recovered from the Faeces of Dairy
RT Cattle.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:KRW62624.1}.
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DR EMBL; LKKK01000001; KRW62624.1; -; Genomic_DNA.
DR RefSeq; WP_058066778.1; NZ_LKKK01000001.1.
DR AlphaFoldDB; A0A0T6UXC0; -.
DR STRING; 1729724.AO726_04190; -.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000051864; Unassembled WGS sequence.
DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000051864};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRW62624.1}.
FT DOMAIN 11..258
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 290..367
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 374 AA; 40513 MW; EACADE091EC0E19C CRC64;
MTSATLAKTP LHALHLELGA RMVPFAGYDM PVQYPLGVLK EHLHTREQAG LFDVSHMGQI
MLRGPKAAEA LEHLVPVDII DLPVGMQRYA MFTDTNGGIL DDLMVANLGN DTLFLVVNAA
CKDQDLAHLQ KHIGDQCEII DFFESRALLA LQGPKAAEVL ARLAPEVTKM TFMQFTQVRL
LGVDCYVSRS GYTGEDGYEI SVPNQQAETL ARSLLAEPEV QPIGLGARDS LRLEAGLCLY
GHDMSNETTP IEASLLWAIS KPRRADGARA GGFPGAKRIF EQQQEGVPSK RVGLLPQERV
PVREGAEIVA ADGEVIGKVT SGGFGPTLGA PVAMGYVSVS HSAVDTDVWA IVRGKRVAMK
VAKTPFVPQR YYRG
//
