(data stored in ACNUC7421 zone)

SWISSPROT: Q13E13_RHOPS

ID   Q13E13_RHOPS            Unreviewed;       221 AA.
AC   Q13E13;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 69.
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=RPD_0438 {ECO:0000313|EMBL:ABE37676.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37676.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37676.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37676.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) 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; CP000283; ABE37676.1; -; Genomic_DNA.
DR   STRING; 316057.RPD_0438; -.
DR   EnsemblBacteria; ABE37676; ABE37676; RPD_0438.
DR   KEGG; rpd:RPD_0438; -.
DR   eggNOG; ENOG4105DFA; Bacteria.
DR   eggNOG; COG0325; LUCA.
DR   HOGENOM; HOG000048981; -.
DR   KO; K06997; -.
DR   OMA; LQWHFIG; -.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.10; -; 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   PANTHER; PTHR10146; PTHR10146; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PIRSF; PIRSF004848; YBL036c_PLPDEIII; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00044; TIGR00044; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13E13.
DR   SWISS-2DPAGE; Q13E13.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02087,
KW   ECO:0000256|PIRSR:PIRSR004848-1}.
FT   DOMAIN       14    220       Ala_racemase_N. {ECO:0000259|Pfam:
FT                                PF01168}.
FT   MOD_RES      37     37       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02087,
FT                                ECO:0000256|PIRSR:PIRSR004848-1}.
SQ   SEQUENCE   221 AA;  23335 MW;  C213C29F196B6318 CRC64;
     MSGAEVHGLA AVEQEIAQAC KEARRERGSV TLIAVSKTFD ADSILPVLAA GQRVFGENRV
     QEAKAKWPAL VAGHPGTELH LIGPLQSNKA KEAVALFDAI HSVDRESLAE ALSKALPLAG
     RAVELFVQIN TGEEPQKAGV APQDADAFLT ACRERWGLTI AGLMCIPPVD EAPAPHFALT
     AKIARRNGLS KLSMGMSADF ATAIEFGATH VRVGSAIFGH R
//

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