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Database: UniProt
Entry: I8UDY6_9BACI
LinkDB: I8UDY6_9BACI
Original site: I8UDY6_9BACI 
ID   I8UDY6_9BACI            Unreviewed;       225 AA.
AC   I8UDY6;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=A374_11940 {ECO:0000313|EMBL:EIT85008.1};
OS   Fictibacillus macauensis ZFHKF-1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX   NCBI_TaxID=1196324 {ECO:0000313|EMBL:EIT85008.1, ECO:0000313|Proteomes:UP000004080};
RN   [1] {ECO:0000313|EMBL:EIT85008.1, ECO:0000313|Proteomes:UP000004080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZFHKF-1 {ECO:0000313|EMBL:EIT85008.1,
RC   ECO:0000313|Proteomes:UP000004080};
RX   PubMed=22887677; DOI=10.1128/JB.01049-12;
RA   Cai L., Zhang T.;
RT   "Genome of Bacillus macauensis ZFHKF-1, a Long-Chain-Forming Bacterium.";
RL   J. Bacteriol. 194:4780-4780(2012).
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:EIT85008.1}.
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DR   EMBL; AKKV01000027; EIT85008.1; -; Genomic_DNA.
DR   RefSeq; WP_007202468.1; NZ_AKKV01000027.1.
DR   AlphaFoldDB; I8UDY6; -.
DR   STRING; 1196324.A374_11940; -.
DR   PATRIC; fig|1196324.3.peg.2443; -.
DR   eggNOG; COG0325; Bacteria.
DR   OrthoDB; 9804072at2; -.
DR   Proteomes; UP000004080; Unassembled WGS sequence.
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.
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:UP000004080}.
FT   DOMAIN          6..222
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         35
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   225 AA;  25275 MW;  3DF937BD07BFBD9D CRC64;
     MDIKQNLQHI KERITTICQE KKRNPEDVKI IAVTKYVSTE TAIQAVSAGV QHIGENRPEG
     LATKYEALPE GITWHFIGSL QTRKVKEILP FVDCIHSLDR ASLAKEIQKR ADRVIDCMVQ
     VNVSGEESKH GISPQELLSF IESMKEYPSI RIVGLMTMAP FTDDQNLLHT VFASMKTLQQ
     EVQDKQFSFA PCTELSMGMS NDYEIAVQEG ATFVRIGTSL VGKEF
//
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