ID A0A090C9E8_PODAN Unreviewed; 345 AA.
AC A0A090C9E8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CDP23451.1, ECO:0000313|Proteomes:UP000001197};
RN [1] {ECO:0000313|EMBL:CDP23451.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
CC -!- SIMILARITY: Belongs to the pyridoxine kinase family.
CC {ECO:0000256|ARBA:ARBA00008805}.
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DR EMBL; FO904936; CDP23451.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090C9E8; -.
DR STRING; 515849.A0A090C9E8; -.
DR eggNOG; KOG2599; Eukaryota.
DR InParanoid; A0A090C9E8; -.
DR Proteomes; UP000001197; Chromosome 1.
DR GO; GO:0008478; F:pyridoxal kinase activity; IEA:UniProtKB-EC.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000001197}.
FT DOMAIN 70..185
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT REGION 286..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 345 AA; 36978 MW; 554E203800F5E638 CRC64;
MQSLGCDVAA LNTVDFSNHT GYGQWTGTRS TPEHILDLWS GLKQSFLDDF DMMLSGYVPG
AEALGAVGRI AEELKSRAEG RFFWVLDPVM GDNGNLYVGG DVVPVYRGLA GKADLCLPNQ
FEAELLSEVK ITDMLSLGKA IEVLHSRYGV PHIVITSLSL PDDTDPDTPG NKKTLSVVGS
SMTSTKQPRA FKISFPAIDC YFSGTGDMFA ALMVVRMREA VCDASTSTEP GLDTRRSWLS
EDGVGALELP LARAAERVLG SMHEVLAKTA EGLEGRLEEM VRGVKTGGVN GNGNGNGNGE
GEGEGEGGVG KKQMQVLKSK AAELKLVRHL DSLRGPKVVF RARRL
//
