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Database: UniProt
Entry: A0A0S8DYN1_9BACT
LinkDB: A0A0S8DYN1_9BACT
Original site: A0A0S8DYN1_9BACT 
ID   A0A0S8DYN1_9BACT        Unreviewed;       225 AA.
AC   A0A0S8DYN1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Pyridoxal phosphate homeostasis protein {ECO:0000256|HAMAP-Rule:MF_02087};
DE            Short=PLP homeostasis protein {ECO:0000256|HAMAP-Rule:MF_02087};
GN   ORFNames=AMJ78_06755 {ECO:0000313|EMBL:KPK40833.1};
OS   Omnitrophica WOR_2 bacterium SM23_29.
OC   Bacteria; Candidatus Omnitrophota.
OX   NCBI_TaxID=1703776 {ECO:0000313|EMBL:KPK40833.1, ECO:0000313|Proteomes:UP000050824};
RN   [1] {ECO:0000313|EMBL:KPK40833.1, ECO:0000313|Proteomes:UP000050824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_29 {ECO:0000313|EMBL:KPK40833.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
CC   -!- FUNCTION: Pyridoxal 5'-phosphate (PLP)-binding protein, which is
CC       involved in PLP homeostasis. {ECO:0000256|HAMAP-Rule:MF_02087}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR004848-1};
CC   -!- SIMILARITY: Belongs to the pyridoxal phosphate-binding protein
CC       YggS/PROSC family. {ECO:0000256|HAMAP-Rule:MF_02087,
CC       ECO:0000256|RuleBase:RU004514}.
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:KPK40833.1}.
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DR   EMBL; LJUB01000070; KPK40833.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8DYN1; -.
DR   PATRIC; fig|1703776.3.peg.635; -.
DR   Proteomes; UP000050824; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   CDD; cd00635; PLPDE_III_YBL036c_like; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   HAMAP; MF_02087; PLP_homeostasis; 1.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   InterPro; IPR011078; PyrdxlP_homeostasis.
DR   NCBIfam; TIGR00044; YggS family pyridoxal phosphate-dependent enzyme; 1.
DR   PANTHER; PTHR10146; PROLINE SYNTHETASE CO-TRANSCRIBED BACTERIAL HOMOLOG PROTEIN; 1.
DR   PANTHER; PTHR10146:SF14; PYRIDOXAL PHOSPHATE HOMEOSTASIS PROTEIN; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PIRSF; PIRSF004848; YBL036c_PLPDEIII; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02087,
KW   ECO:0000256|PIRSR:PIRSR004848-1}.
FT   DOMAIN          33..223
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         34
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   225 AA;  25070 MW;  6C6380F6125514CD CRC64;
     MIYENLMHVR QRIGEAAGRG GRNGDEIVLV CVTKGVGITQ IEEAVKAGVT DIGENYIQDA
     VKKFNAIGRK VKWHFIGHLQ TNKVKDAVYI FDLIHSVDSL KLAQEISRQA SKLGIIKDVL
     IEVKTSEEAT KYGILPAGVS NLIEEVSTLP NLRVMGLMTM APIVDTPEKA RPYFRRLKEL
     SQAIATKKIE NVRMQWLSMG MTQDFEVAIE ESANMVRIGR AIFEG
//
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