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Database: UniProt
Entry: A0A178KPY0_9GAMM
LinkDB: A0A178KPY0_9GAMM
Original site: A0A178KPY0_9GAMM 
ID   A0A178KPY0_9GAMM        Unreviewed;       236 AA.
AC   A0A178KPY0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=A3K86_00140 {ECO:0000313|EMBL:OAN19439.1};
OS   Photobacterium jeanii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=858640 {ECO:0000313|EMBL:OAN19439.1, ECO:0000313|Proteomes:UP000078503};
RN   [1] {ECO:0000313|EMBL:OAN19439.1, ECO:0000313|Proteomes:UP000078503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R-40508 {ECO:0000313|EMBL:OAN19439.1,
RC   ECO:0000313|Proteomes:UP000078503};
RA   Li Y.;
RT   "Photobacterium proteolyticum sp. nov. a protease producing bacterium
RT   isolated from ocean sediments of Laizhou Bay.";
RL   Submitted (MAR-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAN19439.1}.
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DR   EMBL; LVHF01000008; OAN19439.1; -; Genomic_DNA.
DR   RefSeq; WP_068325823.1; NZ_PYMD01000012.1.
DR   AlphaFoldDB; A0A178KPY0; -.
DR   STRING; 858640.A3K86_00140; -.
DR   OrthoDB; 9804072at2; -.
DR   Proteomes; UP000078503; Unassembled WGS sequence.
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:UP000078503}.
FT   DOMAIN          28..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   236 AA;  25668 MW;  FF05159EF307D9A2 CRC64;
     MSSIKQNIEQ VITQIASATE KCGRDADSVQ LLAVSKTKPI AAIQEAIEAG HFAFGENYVQ
     EGVEKVQHFR DTDHSAALQW HFIGPIQSNK TRPIAEHFDW VHSIDRVKIA RRLSEQRPAN
     SAPLQVLLQV NTSNEASKSG LIFAELPQAA ADIAQMPNIE LRGLMSIPEK ANDYDSQFAA
     FHALAEAMNT LKADHPQLDT LSMGMSGDMD AAIAAGSTIV RIGTAIFGAR DYSNKA
//
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