(data stored in SCRATCH zone)

SWISSPROT: A0A0E1NTA5_YERPA

ID   A0A0E1NTA5_YERPA        Unreviewed;       232 AA.
AC   A0A0E1NTA5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   05-DEC-2018, entry version 22.
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=YPA_0324 {ECO:0000313|EMBL:ABG12292.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12292.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12292.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12292.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02087}.
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; CP000308; ABG12292.1; -; Genomic_DNA.
DR   RefSeq; WP_002215609.1; NZ_CP009906.1.
DR   EnsemblBacteria; ABG12292; ABG12292; YPA_0324.
DR   EnsemblBacteria; AJJ80150; AJJ80150; CH58_3172.
DR   KEGG; ypa:YPA_0324; -.
DR   PATRIC; fig|360102.15.peg.3328; -.
DR   KO; K06997; -.
DR   OMA; LQWHFIG; -.
DR   BioCyc; YPES360102:GHZU-343-MONOMER; -.
DR   Proteomes; UP000001971; 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.
DR   PROSITE; PS01211; UPF0001; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0E1NTA5.
DR   SWISS-2DPAGE; A0A0E1NTA5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02087,
KW   ECO:0000256|PIRSR:PIRSR004848-1}.
FT   MOD_RES      36     36       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_02087,
FT                                ECO:0000256|PIRSR:PIRSR004848-1}.
SQ   SEQUENCE   232 AA;  25310 MW;  2B450D8A415DB818 CRC64;
     MSTIQQNLQD VRARIATAAH NCGRSPEEVT LLAVSKTKPV AAIEKAIAAG QYAFGENYVQ
     EGVDKIHSFV DNKTLEWHFI GPLQSNKSRL VAENFAWCHT VDRLKIAQRL SAQRPAAMPA
     LNVLIQINIS DEQSKAGISL SELPALADSI STLPNLCLRG LMAIPAPEHD YQRQLAVFTQ
     MNQAFLTLKA RYPQIDTLSM GMTDDMDAAI SAGSTLVRIG TAIFGARVYN AD
//

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