(data stored in SCRATCH zone)

SWISSPROT: Q6BM15_DEBHA

ID   Q6BM15_DEBHA            Unreviewed;       861 AA.
AC   Q6BM15;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   08-MAY-2019, entry version 90.
DE   RecName: Full=Histidine biosynthesis trifunctional protein {ECO:0000256|PIRNR:PIRNR001257};
DE   Includes:
DE     RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000256|PIRNR:PIRNR001257};
DE              EC=3.5.4.19 {ECO:0000256|PIRNR:PIRNR001257};
DE   Includes:
DE     RecName: Full=Phosphoribosyl-ATP pyrophosphohydrolase {ECO:0000256|PIRNR:PIRNR001257};
DE              EC=3.6.1.31 {ECO:0000256|PIRNR:PIRNR001257};
DE   Includes:
DE     RecName: Full=Histidinol dehydrogenase {ECO:0000256|PIRNR:PIRNR001257};
DE              Short=HDH {ECO:0000256|PIRNR:PIRNR001257};
DE              EC=1.1.1.23 {ECO:0000256|PIRNR:PIRNR001257};
GN   OrderedLocusNames=DEHA2F09086g {ECO:0000313|EMBL:CAG89097.1};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG89097.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG89097.1, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-
CC         beta-D-ribosyl)-5-[(5-phospho-beta-D-
CC         ribosylamino)methylideneamino]imidazole-4-carboxamide;
CC         Xref=Rhea:RHEA:20049, ChEBI:CHEBI:15377, ChEBI:CHEBI:58435,
CC         ChEBI:CHEBI:59457; EC=3.5.4.19;
CC         Evidence={ECO:0000256|PIRNR:PIRNR001257};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-
CC         beta-D-ribosyl)-5'-AMP + diphosphate + H(+);
CC         Xref=Rhea:RHEA:22828, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:59457, ChEBI:CHEBI:73183;
CC         EC=3.6.1.31; Evidence={ECO:0000256|PIRNR:PIRNR001257};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2
CC         NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595,
CC         ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23;
CC         Evidence={ECO:0000256|PIRNR:PIRNR001257};
CC   -!- SIMILARITY: In the C-terminal section; belongs to the histidinol
CC       dehydrogenase family. {ECO:0000256|PIRNR:PIRNR001257}.
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DR   EMBL; CR382138; CAG89097.1; -; Genomic_DNA.
DR   RefSeq; XP_460756.1; XM_460756.1.
DR   STRING; 4959.XP_460756.1; -.
DR   EnsemblFungi; CAG89097; CAG89097; DEHA2F09086g.
DR   GeneID; 2903773; -.
DR   KEGG; dha:DEHA2F09086g; -.
DR   HOGENOM; HOG000243914; -.
DR   InParanoid; Q6BM15; -.
DR   KO; K14152; -.
DR   OMA; CGDYSSG; -.
DR   OrthoDB; 313644at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06572; Histidinol_dh; 1.
DR   Gene3D; 3.10.20.400; -; 1.
DR   HAMAP; MF_01024; HisD; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR008179; HisE.
DR   InterPro; IPR016298; Histidine_synth_trifunct.
DR   InterPro; IPR001692; Histidinol_DH_CS.
DR   InterPro; IPR012131; Hstdl_DH.
DR   InterPro; IPR021130; PRib-ATP_PPHydrolase-like.
DR   InterPro; IPR002496; PRib_AMP_CycHydrolase_dom.
DR   InterPro; IPR038019; PRib_AMP_CycHydrolase_sf.
DR   PANTHER; PTHR21256; PTHR21256; 1.
DR   Pfam; PF00815; Histidinol_dh; 1.
DR   Pfam; PF01502; PRA-CH; 1.
DR   Pfam; PF01503; PRA-PH; 1.
DR   PIRSF; PIRSF001257; His_trifunctional; 1.
DR   PRINTS; PR00083; HOLDHDRGNASE.
DR   ProDom; PD002610; PRA_CycHdrlase; 1.
DR   SUPFAM; SSF141734; SSF141734; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   TIGRFAMs; TIGR00069; hisD; 1.
DR   TIGRFAMs; TIGR03188; histidine_hisI; 1.
DR   PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BM15.
DR   SWISS-2DPAGE; Q6BM15.
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR001257};
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR001257};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Histidine biosynthesis {ECO:0000256|PIRNR:PIRNR001257};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001257};
KW   NAD {ECO:0000256|PIRNR:PIRNR001257};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001257};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR001257};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599}.
FT   DOMAIN      212    287       PRA-CH. {ECO:0000259|Pfam:PF01502}.
FT   COILED      333    353       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   861 AA;  94020 MW;  C7235E89D54845CE CRC64;
     MTFPILPIIS SSNKEAIAEF SVVGQILLPL ESVSISKHFL HQFPNYIDVN VDTTSSKVDI
     DQIVELLNSG IKQVFIKESQ IEEFILSGGL PSSRFAIKFD SSKVSDTALE TDSAFVFNCE
     LAKDDAKKYS QSGNRGLYYE NPSITQELAN KLATEDIYPI IASESLTTAS SESGKISISS
     LFTAGLTTDR PDGLFTTLIT TPAPSYTALG IVYSSVESIH ASIAEKQGVY QSRKRRDELW
     YKGKTSGATQ KLVKLEKDCD SDVVKFIVEP REGYGFCHLD KNFTCFHDGE LKQKGESFGK
     GLARLDNTLQ DRFQSAPEGS YTKRLFNDEP LLIAKLKEEL DELIEAGQSS SKDTNEVAWE
     CADLFYFAMV WCIKNGVRLA DVERNLDIKS GKVTRRKGDA KPAYLKTDNE KSEQSNEEYK
     METIYVNDKT TDPKDIAKAL NRPVQKTADI MKLVLPIIDK VKKDGDKALL ELTSKFDGVK
     LKSPVLSAPF PADLMDISEE MKEAIDLSMT NIEKFHAAQL PKEKIMTVET APGVYCSRFA
     KAIENVGLYV PGGTAVLPST AMMLGVPAKV AGCSNIIVAT PPSRSTGKLT PEVVYVAHKL
     GAKCIVMAGG AQAVTAMAYG TESVLKCDKI LGPGNQFVTA AKMHVQNDTQ ALCSIDMPAG
     PSEVLVIADS EADADFVASD LLSQAEHGVD SQVILVGVGL TKEKLNEFES AVKKQAQVLP
     RKDIVAKCLS HSYTLLVDTY DEAFKLSNKY APEHLILQVE NARSFVPDYI ENAGSVFVGG
     LSPESCGDYS SGTNHTLPTY GYARQYSGVN TATFQKFITS QDVTEEGLKS IGKAVMTLAE
     VEGLEAHRNA VHVRMEKLGL L
//

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