GenomeNet

Database: UniProt
Entry: A0A0G3CKG0_9GAMM
LinkDB: A0A0G3CKG0_9GAMM
Original site: A0A0G3CKG0_9GAMM 
ID   A0A0G3CKG0_9GAMM        Unreviewed;       233 AA.
AC   A0A0G3CKG0;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=QQ39_03055 {ECO:0000313|EMBL:AKJ41185.1};
OS   Pragia fontium.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Budviciaceae; Pragia.
OX   NCBI_TaxID=82985 {ECO:0000313|EMBL:AKJ41185.1, ECO:0000313|Proteomes:UP000068021};
RN   [1] {ECO:0000313|EMBL:AKJ41185.1, ECO:0000313|Proteomes:UP000068021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=24613 {ECO:0000313|EMBL:AKJ41185.1,
RC   ECO:0000313|Proteomes:UP000068021};
RX   PubMed=26159528;
RA   Snopkova K., Sedlar K., Bosak J., Chaloupkova E., Provaznik I., Smajs D.;
RT   "Complete Genome Sequence of Pragia fontium 24613, an Environmental
RT   Bacterium from the Family Enterobacteriaceae.";
RL   Genome Announc. 3:e00740-15(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   -!- 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP010423; AKJ41185.1; -; Genomic_DNA.
DR   RefSeq; WP_047779928.1; NZ_CP010423.1.
DR   AlphaFoldDB; A0A0G3CKG0; -.
DR   STRING; 82985.QQ39_03055; -.
DR   KEGG; pfq:QQ39_03055; -.
DR   PATRIC; fig|82985.3.peg.634; -.
DR   OrthoDB; 9804072at2; -.
DR   Proteomes; UP000068021; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   CDD; cd06824; PLPDE_III_Yggs_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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000068021}.
FT   DOMAIN          7..230
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         36
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   233 AA;  25989 MW;  623E359808420E1D CRC64;
     MTTIQQNLAA VRQKIAVAAQ QCDRSPEEVQ LLAVSKTKPV AAIQEAIDAG QRQFGENYVQ
     EGVDKIAHFN TTPFANQLEW HFIGPLQSNK SRLVAEHFHW MHTLDREKIA HRLNEQRPAD
     MPPLNVLIQI NISDEQSKSG ISLTELPQLA QQISQLPNLV FRGLMTIPAP EPDPARQLAV
     FQQMTQAFNQ LKSEHPQIDT LSMGMTDDMA NAIRAGSTMV RIGTAIFGAR DYA
//
DBGET integrated database retrieval system