(data stored in ACNUC7421 zone)

SWISSPROT: A2Q8P2_ASPNC

ID   A2Q8P2_ASPNC            Unreviewed;       367 AA.
AC   A2Q8P2;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 66.
DE   SubName: Full=Aspergillus niger contig An01c0170, genomic contig {ECO:0000313|EMBL:CAK37039.1};
DE            EC=2.7.1.35 {ECO:0000313|EMBL:CAK37039.1};
GN   ORFNames=An01g05050 {ECO:0000313|EMBL:CAK37039.1};
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011 {ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK37039.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 {ECO:0000313|Proteomes:UP000006706};
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA   Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA   van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA   Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA   Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA   Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA   van Ooyen A.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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DR   EMBL; AM269964; CAK37039.1; -; Genomic_DNA.
DR   RefSeq; XP_001388931.1; XM_001388894.2.
DR   PaxDb; A2Q8P2; -.
DR   EnsemblFungi; CAK37039; CAK37039; An01g05050.
DR   GeneID; 4978204; -.
DR   KEGG; ang:ANI_1_2510014; -.
DR   HOGENOM; HOG000258174; -.
DR   KO; K00868; -.
DR   Proteomes; UP000006706; Chromosome 2R.
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; PTHR10534; 1.
DR   Pfam; PF08543; Phos_pyr_kin; 1.
DR   SUPFAM; SSF53613; SSF53613; 1.
DR   TIGRFAMs; TIGR00687; pyridox_kin; 1.
PE   4: Predicted;
DR   PRODOM; A2Q8P2.
DR   SWISS-2DPAGE; A2Q8P2.
KW   Transferase {ECO:0000313|EMBL:CAK37039.1}.
FT   DOMAIN          116..247
FT                   /note="Phos_pyr_kin"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   367 AA;  40356 MW;  6D1489AF096FC3CA CRC64;
     MSADLLVPET RVLAVASHVV YGYVGNKMAS AVMQLMGCDV AALNTVHFSN HTGYRQFKGT
     RATAEEITAL YEGLTQSNLL DFDVMLSGYA PSAAAVEAVG AIGMDLQRKA EKNPGSFFWV
     LDPVMGDQGR LYVNDDVVPA YKKVIRHADL ILPNQFEAEV LSGIKITSLA TLAEAITALH
     AIYNIPHVII TSVQIASLSD SPLPNTLTVI GSTTRSDGAP RLFRIDVPAL DCYFSGTGDM
     FAALTVARFR EAVFNADPTL RNTKSWVSPD NVPATELPLA QSTRKVLASM HCVLEKTLEA
     RDAELRAIVP DESEKLLSQE DQQKRAHLRE SKAAEVRVVR HAQYLREPEV EFQASEWRRE
     DLPAQFR
//

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