GenomeNet

Database: UniProt
Entry: W2DXC4_9PSED
LinkDB: W2DXC4_9PSED
Original site: W2DXC4_9PSED 
ID   W2DXC4_9PSED            Unreviewed;       360 AA.
AC   W2DXC4;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
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:ETK24023.1};
GN   ORFNames=H096_07757 {ECO:0000313|EMBL:ETK24023.1};
OS   Pseudomonas sp. FH1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1284392 {ECO:0000313|EMBL:ETK24023.1, ECO:0000313|Proteomes:UP000018863};
RN   [1] {ECO:0000313|EMBL:ETK24023.1, ECO:0000313|Proteomes:UP000018863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FH1 {ECO:0000313|EMBL:ETK24023.1,
RC   ECO:0000313|Proteomes:UP000018863};
RX   PubMed=24286439; DOI=10.1111/1462-2920.12345;
RA   Rhodes G., Bosma H., Studholme D., Arnold D.L., Jackson R.W., Pickup R.W.;
RT   "The rulB gene of plasmid pWW0 is a hotspot for the site-specific insertion
RT   of integron-like elements found in the chromosomes of environmental
RT   Pseudomonas fluorescens group bacteria.";
RL   Environ. Microbiol. 16:2374-2388(2014).
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}.
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:ETK24023.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AOHM01000020; ETK24023.1; -; Genomic_DNA.
DR   RefSeq; WP_033897549.1; NZ_AOHM01000020.1.
DR   AlphaFoldDB; W2DXC4; -.
DR   PATRIC; fig|1284392.3.peg.1525; -.
DR   Proteomes; UP000018863; Unassembled WGS sequence.
DR   GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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   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   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}; Methyltransferase {ECO:0000313|EMBL:ETK24023.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00259}.
FT   DOMAIN          7..252
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          280..353
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   360 AA;  39681 MW;  A7E5A1B3F5EFE245 CRC64;
     MGQRTPLYDL HLALGAKMVD FGGWDMPLHY GSQVEEHHQV RRDCGVFDVS HMTVIDVTGP
     QAKEWLQYLL ANDVERLHGC GRALYSAMLN EKGGVVDDMI VYRTESAYRL VVNAATRDQD
     MAWMHAQLGN YQVQLHERPE LAMLAIQGPH ARQKIAELVT QSRGALIHQL KPFEGQADGD
     WFIARTGYTG EDGLEIVLPA DQAPGFFNDL VGAGISPIGL GARDTLRLEA GMNLYGQDIH
     QDVSPLASNM AWSIAWEPAE RNFIGRAALE AEKAAGVQFK LVGLVLEERG VLRAHQVVRI
     ANIGEGEITS GSFSPTLSKS IALARVPTAT ADRAEVEIRG KWYPVRVVKP TFVRHGKTLI
//
DBGET integrated database retrieval system