GenomeNet

Database: UniProt
Entry: S5XYN0_PARAH
LinkDB: S5XYN0_PARAH
Original site: S5XYN0_PARAH 
ID   S5XYN0_PARAH            Unreviewed;       369 AA.
AC   S5XYN0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
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   ORFNames=JCM7686_3377 {ECO:0000313|EMBL:AGT10412.1};
OS   Paracoccus aminophilus JCM 7686.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1367847 {ECO:0000313|EMBL:AGT10412.1, ECO:0000313|Proteomes:UP000015480};
RN   [1] {ECO:0000313|EMBL:AGT10412.1, ECO:0000313|Proteomes:UP000015480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 7686 {ECO:0000313|EMBL:AGT10412.1};
RX   PubMed=24517536; DOI=10.1186/1471-2164-15-124;
RA   Dziewit L., Czarnecki J., Wibberg D., Radlinska M., Mrozek P., Szymczak M.,
RA   Schluter A., Puhler A., Bartosik D.;
RT   "Architecture and functions of a multipartite genome of the methylotrophic
RT   bacterium Paracoccus aminophilus JCM 7686, containing primary and secondary
RT   chromids.";
RL   BMC Genomics 15:124-124(2014).
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   ---------------------------------------------------------------------------
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; CP006650; AGT10412.1; -; Genomic_DNA.
DR   RefSeq; WP_020952048.1; NC_022041.1.
DR   AlphaFoldDB; S5XYN0; -.
DR   STRING; 1367847.JCM7686_3377; -.
DR   KEGG; pami:JCM7686_3377; -.
DR   PATRIC; fig|1367847.3.peg.3409; -.
DR   eggNOG; COG0404; Bacteria.
DR   HOGENOM; CLU_007884_10_0_5; -.
DR   OrthoDB; 9774591at2; -.
DR   Proteomes; UP000015480; Chromosome.
DR   GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
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   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   Methyltransferase {ECO:0000313|EMBL:AGT10412.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015480};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGT10412.1}.
FT   DOMAIN          9..252
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          284..362
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   369 AA;  39326 MW;  87CAB901B5A80D80 CRC64;
     MAENRRTTLY DLHLARGAKM VPFAGWDMPV QYPMGVLNEH LHTRAKAGLF DVSHMGQVIL
     RGPEVAVALE SLIPADLAGL KPGRQRYGLF TAENGGVLDD LMIANKGDHL YLVVNAANAE
     ADLAHLRQLE GKGISVEPQD RALLALQGPE AAAVLARLIP GVAEMTFMDS RDFDWQGVDL
     WISRSGYTGE DGFEISVPQA RAVALAEALL ANEAVAPIGL GARDSLRLEA GMPLYGHEMD
     EMTSPAQASL GWSIPKIRRL GGARAGGFPG AERVLAELAA GATRARYGLR PEGRAPIREG
     VEIFAEETGG TAIGRVRSGG FGPSVGAPIA MADLPAGLSP DTPLWAELRG RRLPVAITPL
     PFHTPAYKR
//
DBGET integrated database retrieval system