ID A0A1B3W5E3_9GAMM Unreviewed; 368 AA.
AC A0A1B3W5E3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:AOH35283.1};
GN ORFNames=BGP89_02040 {ECO:0000313|EMBL:AOH35283.1};
OS Luteimonas sp. JM171.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Luteimonas.
OX NCBI_TaxID=1896164 {ECO:0000313|EMBL:AOH35283.1, ECO:0000313|Proteomes:UP000095036};
RN [1] {ECO:0000313|Proteomes:UP000095036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JM171 {ECO:0000313|Proteomes:UP000095036};
RA Wan X., Miller J.M., Rowley S.J., Hou S., Donachie S.P.;
RT "Draft genome sequence of a novel Luteimonas sp. from coral mucus,
RT Hawaii.";
RL Submitted (AUG-2016) 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}.
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DR EMBL; CP017074; AOH35283.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B3W5E3; -.
DR STRING; 1896164.BGP89_02040; -.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000095036; Chromosome.
DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-UniRule.
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 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000095036};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00259}.
FT DOMAIN 7..259
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 285..357
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 368 AA; 39994 MW; DACF010800B45C8D CRC64;
MTRKTVLNDT HRALGAKMVD FGGWDMPLNY GSQMEEHHHV RRAAGMFDVS HMTVIDLSGP
QARDFLRRLL ANSIDKLKKP GKALYSCMLN EQGGVIDDLI VYLLGEGEYR IVSNAATRDK
DLAWIQRHAK DFDVQVRERP ELAIIAVQGP QAREAVLGLV ADGDRGRVDA LGRFSALDAK
SADGVDLFIA RTGYTGEDGF EIVLPEAGAV AFWNALIEAG VKPAGLAARD TLRLEAGMNL
YGQDMDEDVT PYVAGLGWTV SLDEGRDFIG RQALEAQKAD GVPHQLVGLV MDGRGVLRHG
QRVLSDAGEG QILSGTFSPT IGKAIAFARI PAGEPGEVRV DLRGREVPLR IVRHPFVREG
QVQPGVAE
//
