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Database: UniProt
Entry: B8DQN2_DESVM
LinkDB: B8DQN2_DESVM
Original site: B8DQN2_DESVM 
ID   B8DQN2_DESVM            Unreviewed;       272 AA.
AC   B8DQN2;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
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   OrderedLocusNames=DvMF_2208 {ECO:0000313|EMBL:ACL09151.1};
OS   Desulfovibrio vulgaris (strain DSM 19637 / Miyazaki F).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Nitratidesulfovibrio.
OX   NCBI_TaxID=883 {ECO:0000313|EMBL:ACL09151.1};
RN   [1] {ECO:0000313|EMBL:ACL09151.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Miyazaki F {ECO:0000313|EMBL:ACL09151.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hazen T.C.,
RA   Richardson P.;
RT   "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP001197; ACL09151.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8DQN2; -.
DR   STRING; 883.DvMF_2208; -.
DR   KEGG; dvm:DvMF_2208; -.
DR   eggNOG; COG0325; Bacteria.
DR   HOGENOM; CLU_059988_0_1_7; -.
DR   OrthoDB; 9804072at2; -.
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.
DR   PROSITE; PS01211; UPF0001; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02087,
KW   ECO:0000256|PIRSR:PIRSR004848-1}.
FT   DOMAIN          26..269
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         52
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   272 AA;  28496 MW;  FD54F47BB0CDBA8F CRC64;
     MPHDIAAASA FLPPEAAQSL LDRWAAVRAR VDGAARAAGR DPAGVTLVAV SKFHPAASVA
     ALSAAGQRDF GENYVQEALR KQAEVADMTG MGPDAASGTK VAGGAAPRWH FIGHLQSNKA
     KDVVGRFALL HTVDSEALAR KLDQRLSGMP AQGAGGVAPG QDILLQVNIG DEEQKSGVDP
     DDLPALTDAV LALPRLRLLG LMCMPPIFDD GEASRPYFAR LRELRDALSA RVGLPLPHLS
     MGMSHDVEVA VAEGATIVRV GTDIFGPRPA RL
//
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