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Database: UniProt
Entry: A0A171A483_9BACT
LinkDB: A0A171A483_9BACT
Original site: A0A171A483_9BACT 
ID   A0A171A483_9BACT        Unreviewed;       365 AA.
AC   A0A171A483;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
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   ORFNames=PJIAN_3587 {ECO:0000313|EMBL:GAT63270.1};
OS   Paludibacter jiangxiensis.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Paludibacteraceae;
OC   Paludibacter.
OX   NCBI_TaxID=681398 {ECO:0000313|EMBL:GAT63270.1, ECO:0000313|Proteomes:UP000076586};
RN   [1] {ECO:0000313|Proteomes:UP000076586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NM7 {ECO:0000313|Proteomes:UP000076586};
RA   Qiu Y., Matsuura N., Ohashi A., Tourlousse M.D., Sekiguchi Y.;
RT   "Draft genome sequence of Paludibacter jiangxiensis strain NM7.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000076586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NM7 {ECO:0000313|Proteomes:UP000076586};
RA   Qiu Y.-L., Tourlousse D.M., Matsuura N., Ohashi A., Sekiguchi Y.;
RT   "Draft genome sequence of Paludibacter jiangxiensis NM7(T), a propionate-
RT   producing fermentative bacterium.";
RL   Genome Announc. 0:0-0(2017).
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:GAT63270.1}.
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DR   EMBL; BDCR01000003; GAT63270.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A171A483; -.
DR   STRING; 681398.PJIAN_3587; -.
DR   Proteomes; UP000076586; 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:GAT63270.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076586};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00259}.
FT   DOMAIN          9..257
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          283..361
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   365 AA;  39957 MW;  B3F55BC1E390FE45 CRC64;
     MIKTTPFTEK HIALGAKMAA FAGYNMPIEY SGITDEHMTV RQGVGVFDVS HMGEFWVKGE
     KALPFLQRIT SNDVSVLPVG KAQYSCFPNG KGGIVDDLLV YHYEPQKYML VVNAANIDKD
     WNWCVQNNTE GADLENASDR MAQLAVQGPK AVEVLQKLTA VDLSSIAYYA FTTGEFAGVK
     DVIISNTGYT GAGGFELYFY PEQADIIWNA IFETGKEYGI KPIGLGARDT LRLEMGFALY
     GNDIDDTTSP IEAGLGWITK FADDKNFIDR PLLEQQKAEG VSRRLVGFIL TERGIPRHDY
     PIVDAEGRVI GKVTSGTQSP VLKAGVGMGY VEVGFAKPET QIFISIRNKP VAAKVVKPPF
     CKGAL
//
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