ID D4CZM2_TRIVH Unreviewed; 303 AA.
AC D4CZM2;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 13-SEP-2023, entry version 47.
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=TRV_00264 {ECO:0000313|EMBL:EFE44891.1};
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE44891.1, ECO:0000313|Proteomes:UP000008383};
RN [1] {ECO:0000313|Proteomes:UP000008383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(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 -!- SIMILARITY: Belongs to the pyridoxal phosphate-binding protein
CC YggS/PROSC family. {ECO:0000256|HAMAP-Rule:MF_03225,
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:EFE44891.1}.
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DR EMBL; ACYE01000016; EFE44891.1; -; Genomic_DNA.
DR RefSeq; XP_003025502.1; XM_003025456.1.
DR AlphaFoldDB; D4CZM2; -.
DR GeneID; 9581739; -.
DR KEGG; tve:TRV_00264; -.
DR HOGENOM; CLU_059988_2_0_1; -.
DR OrthoDB; 21261at2759; -.
DR Proteomes; UP000008383; 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 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}.
FT DOMAIN 66..296
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT REGION 31..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03225"
SQ SEQUENCE 303 AA; 32808 MW; 7CCF2B83E4BE6E6F CRC64;
MSTAVGEDMS APTRASVLIA NLSAVSKRIA AASNSRNNHN ETSPSPSAGP VAATSTSDSN
NNNSSAAPPV RLVAVSKLKP VSDILALHSP PTSHLHFGEN YMQELLEKSK ALPPEIRWHF
IGGLQSNKCV TLAREVRGLW AVESVDTEKK ASLLDKGWGE RAEFKQKEND ANQPLDRRLR
VFVQVNTSGE ENKSGIQPGE PTLELCRFIR ENCPRLKLQG LMTIGAIARS KATTPENENE
DFACLRDTRD MVVEKLSLKG EETLELSMGM SNDFEGAIAM GSNQVRVGST IFGARPPKGE
AKS
//
