ID A0A0D1Z4V9_9PEZI Unreviewed; 382 AA.
AC A0A0D1Z4V9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
GN ORFNames=PV09_01881 {ECO:0000313|EMBL:KIW07982.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW07982.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW07982.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW07982.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the pyridoxine kinase family.
CC {ECO:0000256|ARBA:ARBA00008805}.
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DR EMBL; KN847532; KIW07982.1; -; Genomic_DNA.
DR RefSeq; XP_016217851.1; XM_016354839.1.
DR AlphaFoldDB; A0A0D1Z4V9; -.
DR STRING; 253628.A0A0D1Z4V9; -.
DR GeneID; 27309854; -.
DR VEuPathDB; FungiDB:PV09_01881; -.
DR HOGENOM; CLU_046496_0_0_1; -.
DR InParanoid; A0A0D1Z4V9; -.
DR OrthoDB; 5472295at2759; -.
DR Proteomes; UP000053259; Unassembled WGS sequence.
DR GO; GO:0008478; F:pyridoxal kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IEA:InterPro.
DR CDD; cd01173; pyridoxal_pyridoxamine_kinase; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR004625; PyrdxlKinase.
DR InterPro; IPR029056; Ribokinase-like.
DR NCBIfam; TIGR00687; pyridox_kin; 1.
DR PANTHER; PTHR10534; PYRIDOXAL KINASE; 1.
DR PANTHER; PTHR10534:SF2; PYRIDOXAL KINASE; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:KIW07982.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053259};
KW Transferase {ECO:0000313|EMBL:KIW07982.1}.
FT DOMAIN 42..197
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT REGION 201..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 382 AA; 41872 MW; CC655B1C3DD91D63 CRC64;
MLNMSALPET KVLAIASHVS YGYVGNTMAT FVMQSLGAEV SAINTVCYSN HTAYKQVKGR
KVPAEEILDL YEGLKQSFLT DFNVLLSGYV PSAEAVEAVG KIARDLKHES NRKPGSFFWV
LDPVMGDNGK LYIPESEVPA YKSLLRYADL ILPNQFEAEL LSEVKITNLS TLATAIKALH
TRYNTPHIII TSLRLSKVSG RTLPGTTAGN TTHAEEEDDD DVLSVIGSSS TSKGEPRLWR
IDIPAYPVFF SGTGDMFAAL MVVRLREAAA AAGLLNTSSW RSPDDVPATE TPLAKAATKV
LASMQSILGK TYQYYKTEVS EINTRCERAG KCECEDATKA EEMRMHLKKT KAAEVRVVRN
AKDLIEPSDL DKYAAKAVEV EF
//
