ID A0A089WK61_9PSED Unreviewed; 373 AA.
AC A0A089WK61;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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:AIR89650.1};
GN ORFNames=LK03_10280 {ECO:0000313|EMBL:AIR89650.1};
OS Pseudomonas cremoricolorata.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=157783 {ECO:0000313|EMBL:AIR89650.1, ECO:0000313|Proteomes:UP000029493};
RN [1] {ECO:0000313|EMBL:AIR89650.1, ECO:0000313|Proteomes:UP000029493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND07 {ECO:0000313|EMBL:AIR89650.1,
RC ECO:0000313|Proteomes:UP000029493};
RA Chan K.-G.;
RL Submitted (SEP-2014) 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}.
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DR EMBL; CP009455; AIR89650.1; -; Genomic_DNA.
DR RefSeq; WP_038412225.1; NZ_CP009455.1.
DR AlphaFoldDB; A0A089WK61; -.
DR STRING; 157783.LK03_10280; -.
DR KEGG; psw:LK03_10280; -.
DR eggNOG; COG0404; Bacteria.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000029493; Chromosome.
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:UP000029493};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AIR89650.1}.
FT DOMAIN 10..257
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 288..366
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 373 AA; 40486 MW; 9013AE5484C6C2EC CRC64;
MSDPLRCTPL HTLHLELGAS MVPFAGYDMP VHYPLGVLKE HLHTRAEAGL FDVSHMGQIL
LRGEQAAQAL ERLVPMDIVD LPQGLQRYAL FTNDHGGILD DLMVARLAKD ELLLVVNAAC
KQQDLDYLRQ HLQAHCEVLP QFEERALLAL QGPAAAQVLA QLAPEVAQMT FMQVRPVALL
DAQCFVSRSG YTGEDGFEIS VPATAAKALA RHLLSQPKVQ PIGLGARDSL RLEAGLCLYG
HDMDSDTTPV QANLSWAISK ARRNDGVRAG GFPGAETVFA QQRDGVARKR VGLLVQARSP
VREGAEIVNA AGQAVGQVTS GSFGPTLKAP MAMAYIDNEH TAPDTQLWAV VRGKLVPVRV
SKMPFVASRY QRN
//
