ID Q6CZV4_PECAS Unreviewed; 270 AA.
AC Q6CZV4;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 90.
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=ECA4047 {ECO:0000313|EMBL:CAG76944.1};
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491 {ECO:0000313|EMBL:CAG76944.1, ECO:0000313|Proteomes:UP000007966};
RN [1] {ECO:0000313|EMBL:CAG76944.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SCRI1043 {ECO:0000313|EMBL:CAG76944.1};
RA Bell K.S., Sebaihia M., Pritchard L., Holden M., Hyman L.J., Holeva M.C.,
RA Thomson N.R., Bentley S.D., Churcher C., Mungall K., Atkin R., Bason N.,
RA Brooks K., Chillingworth T., Clark K., Doggett J., Fraser A., Hance Z.,
RA Hauser H., Jagels K., Moule S., Norbertczak H., Ormond D., Price C.,
RA Quail M.A., Sanders M., Walker D., Whitehead S., Salmond G.P.C.,
RA Birch P.R.J., Barrell B.G., Parkhill J., Toth I.K.;
RT "The genome sequence of the enterobacterial phytopathogen Erwinia
RT carotovora subsp. atroseptica SCRI1043 and functional genomic
RT identification of novel virulence factors.";
RL Submitted (FEB-2004) 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 -!- 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; BX950851; CAG76944.1; -; Genomic_DNA.
DR RefSeq; WP_011095523.1; NC_004547.2.
DR AlphaFoldDB; Q6CZV4; -.
DR STRING; 218491.ECA4047; -.
DR GeneID; 57210711; -.
DR KEGG; eca:ECA4047; -.
DR PATRIC; fig|218491.5.peg.4113; -.
DR eggNOG; COG0325; Bacteria.
DR HOGENOM; CLU_059988_1_0_6; -.
DR OrthoDB; 9804072at2; -.
DR Proteomes; UP000007966; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007966}.
FT DOMAIN 29..253
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT MOD_RES 58
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT ECO:0000256|PIRSR:PIRSR004848-1"
SQ SEQUENCE 270 AA; 30144 MW; 94A14277A0460481 CRC64;
MPISSDTPTR HDSHGRYPDA ATVEDFQFNL AAVQMRIAAA CHRVGRDPAT VRLLPVSKTK
PESRLRMAYT AGCRILGENK VQEAYGKWEA MQDLADLQWS VIGHLQTNKA KLVARFASEF
QALDSLRLAE ALDRRLHVEG RSLDVFVQVN TSGEASKYGL SPEDVPAFIQ ALPAFSALRV
RGLMTLALFS SEAERVRQCF IRLRNLRDRL QQNAPVDIRL DELSMGMSGD FEIAIEEGAT
VVRVGQAIFG ARPLPDSYYW PDETTTEVHL
//
