ID G7XJK5_ASPKW Unreviewed; 272 AA.
AC G7XJK5;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=AKAW_05334 {ECO:0000313|EMBL:GAA87220.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA87220.1};
RN [1] {ECO:0000313|EMBL:GAA87220.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA87220.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
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; DF126458; GAA87220.1; -; Genomic_DNA.
DR AlphaFoldDB; G7XJK5; -.
DR STRING; 1033177.G7XJK5; -.
DR VEuPathDB; FungiDB:AKAW_05334; -.
DR eggNOG; KOG3157; Eukaryota.
DR InParanoid; G7XJK5; -.
DR Proteomes; UP000006812; Unassembled WGS sequence.
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 20..264
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT MOD_RES 47
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03225,
FT ECO:0000256|PIRSR:PIRSR004848-1"
SQ SEQUENCE 272 AA; 29862 MW; 1F3D2493E729C537 CRC64;
MTTSIRPSTP TRTTTLLTNL ATVTARINTA TTSSPKTTPP RLVAVSKLKP ASDILTLHTT
NPPTHQTHFG ENYLQELQEK ARLLPTTIKW HFIGGLQSNK CVTLARDTPA LWAVESVDST
KKASLLDKGW GERSAEVKAT NHEERLRVFV QVNTSGEENK SGVEPGDGAL ELCRFIRDKC
PRLRLQGVMT IGAIARSKAT TPENENEDFV CLRETRDRVV KELGLLGEEA KLELSMGMSE
DFEGAIALGS DEVRVGTTIF GDRPPKDQAR VV
//
