ID   A0A1G4JU15_9SACH        Unreviewed;       255 AA.
AC   A0A1G4JU15;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Pyridoxal phosphate homeostasis protein {ECO:0000256|HAMAP-Rule:MF_03225};
DE            Short=PLP homeostasis protein {ECO:0000256|HAMAP-Rule:MF_03225};
GN   ORFNames=LANO_0E06744G {ECO:0000313|EMBL:SCU94428.1};
OS   Lachancea nothofagi CBS 11611.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1266666 {ECO:0000313|EMBL:SCU94428.1};
RN   [1] {ECO:0000313|EMBL:SCU94428.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 11611 {ECO:0000313|EMBL:SCU94428.1};
RA   Devillers H.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Pyridoxal 5'-phosphate (PLP)-binding protein, which may be
CC       involved in intracellular homeostatic regulation of pyridoxal 5'-
CC       phosphate (PLP), the active form of vitamin B6. {ECO:0000256|HAMAP-
CC       Rule:MF_03225}.
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_03225,
CC       ECO:0000256|RuleBase:RU004514}.
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DR   EMBL; LT598451; SCU94428.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4JU15; -.
DR   OrthoDB; 21261at2759; -.
DR   Proteomes; UP000189911; Chromosome e.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   CDD; cd06822; PLPDE_III_YBL036c_euk; 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_03225,
KW   ECO:0000256|PIRSR:PIRSR004848-1}.
FT   DOMAIN          55..248
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         48
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03225,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   255 AA;  28402 MW;  5C16627C13CB9A8E CRC64;
     MLRGIARRTM TDIRQKQLIN SYEAVKSEVM AYAESKGKSD VFLLPVSKLK PASDVQLLYD
     HGVRSFGENY VQELIHKASV LPQDIRWHFI GGLQTNKCKD LAKIPNLYAV ETIDSLKKAV
     KLNEARAKFQ PTAGKILCNV QINTSDEAQK AGLFSDNDIL EVVQFFLSPE ATHVELGGLM
     TIGSWDVSHA ESEENRDFAV LAHWKQVLDA KFSLNLKLSM GMSSDFKQAI NQGTSQVRIG
     TDIFGARPSK AEMRA
//