ID F2S8A2_TRIT1 Unreviewed; 301 AA.
AC F2S8A2;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=TESG_07138 {ECO:0000313|EMBL:EGD99801.1};
OS Trichophyton tonsurans (strain CBS 112818) (Scalp ringworm fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=647933;
RN [1] {ECO:0000313|EMBL:EGD99801.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112818 {ECO:0000313|EMBL:EGD99801.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Henn M., Martinez D., Young S.K., Zeng Q., Gargeya S., Haas B.,
RA Alvarado L., Berlin A., Chapman S., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D., Howarth C.,
RA Larson L., Mehta T., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., White T.C.,
RA Abdel-Rahman S., Graser Y., Gurr S.J., Kohler G., Martinez-Rossi N.,
RA Oliver B.C., Rossi A., Shelest E., Summerbell R., Lander E., Nusbaum C.,
RA Birren B.;
RT "Annotation of Trichophyton tonsurans strain CBS 112818.";
RL Submitted (JUL-2009) 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 -!- 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; GG698526; EGD99801.1; -; Genomic_DNA.
DR AlphaFoldDB; F2S8A2; -.
DR HOGENOM; CLU_059988_2_0_1; -.
DR OrthoDB; 21261at2759; -.
DR Proteomes; UP000009172; 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..294
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT REGION 29..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 75
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03225"
SQ SEQUENCE 301 AA; 32684 MW; DF59584993664F13 CRC64;
MSTAVEEDMS TPTRASVLIA NLSSVSKRIA AASNSRNNHH NETSTSSNPS PAAVTSTSDS
NSPAAPPVRL VAVSKLKPAS DILALHSPPT SHLHFGENYM QELLEKSKAL PPEIRWHFIG
GLQSNKCVTL AREVRGLWAV ESVDTEKKAS LLDKGWGERA EFKQKESEAG EPLDRRLRVF
VQVNTSGEEN KSGIQPGEPT LELCRFIREK CPRLKLQGLM TIGAIARSKA TTPENENEDF
ACLRDTRDMV VEKLSLKGED TLELSMGMSN DFEGAIAMGS SQVRVGSTIF GARPPKGEAK
S
//
