UniProt: A0A0F2LWX6

Database: UniProt
Entry: A0A0F2LWX6_SPOSC

LinkDB:  A0A0F2LWX6_SPOSC 
Original site:  A0A0F2LWX6_SPOSC

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Ontology (7)   
   GO (7)   
Chemical reaction (3)   
   KEGG ENZYME (3)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (12)   
   InterPro (8)   
   Pfam (3)   
   PROSITE (1)   
Literature (2)   
   PubMed (2)   
All databases (28)   

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ID   A0A0F2LWX6_SPOSC        Unreviewed;       873 AA.
AC   A0A0F2LWX6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   13-SEP-2023, entry version 34.
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   ORFNames=SPSK_01021 {ECO:0000313|EMBL:KJR81359.1};
OS   Sporothrix schenckii 1099-18.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX   NCBI_TaxID=1397361 {ECO:0000313|EMBL:KJR81359.1, ECO:0000313|Proteomes:UP000033710};
RN   [1] {ECO:0000313|EMBL:KJR81359.1, ECO:0000313|Proteomes:UP000033710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1099-18 {ECO:0000313|EMBL:KJR81359.1,
RC   ECO:0000313|Proteomes:UP000033710};
RX   PubMed=25351875; DOI=10.1186/1471-2164-15-943;
RA   Teixeira M.M., de Almeida L.G., Kubitschek-Barreira P., Alves F.L.,
RA   Kioshima E.S., Abadio A.K., Fernandes L., Derengowski L.S., Ferreira K.S.,
RA   Souza R.C., Ruiz J.C., de Andrade N.C., Paes H.C., Nicola A.M.,
RA   Albuquerque P., Gerber A.L., Martins V.P., Peconick L.D., Neto A.V.,
RA   Chaucanez C.B., Silva P.A., Cunha O.L., de Oliveira F.F., dos Santos T.C.,
RA   Barros A.L., Soares M.A., de Oliveira L.M., Marini M.M.,
RA   Villalobos-Duno H., Cunha M.M., de Hoog S., da Silveira J.F., Henrissat B.,
RA   Nino-Vega G.A., Cisalpino P.S., Mora-Montes H.M., Almeida S.R.,
RA   Stajich J.E., Lopes-Bezerra L.M., Vasconcelos A.T., Felipe M.S.;
RT   "Comparative genomics of the major fungal agents of human and animal
RT   Sporotrichosis: Sporothrix schenckii and Sporothrix brasiliensis.";
RL   BMC Genomics 15:943-943(2014).
RN   [2] {ECO:0000313|EMBL:KJR81359.1, ECO:0000313|Proteomes:UP000033710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1099-18 {ECO:0000313|EMBL:KJR81359.1,
RC   ECO:0000313|Proteomes:UP000033710};
RX   PubMed=25480940;
RA   Teixeira Mde M., Rodrigues A.M., Tsui C.K., de Almeida L.G.,
RA   Van Diepeningen A.D., van den Ende B.G., Fernandes G.F., Kano R.,
RA   Hamelin R.C., Lopes-Bezerra L.M., Vasconcelos A.T., de Hoog S.,
RA   de Camargo Z.P., Felipe M.S.;
RT   "Asexual propagation of a virulent clone complex in a human and feline
RT   outbreak of sporotrichosis.";
RL   Eukaryot. Cell 14:158-169(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-
CC         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|ARBA:ARBA00000024,
CC         ECO:0000256|PIRNR:PIRNR001257};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-
CC         ribosyl)-5'-AMP + diphosphate + H(+); Xref=Rhea:RHEA:22828,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:59457, ChEBI:CHEBI:73183; EC=3.6.1.31;
CC         Evidence={ECO:0000256|ARBA:ARBA00001460,
CC         ECO:0000256|PIRNR:PIRNR001257};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH;
CC         Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699,
CC         ChEBI:CHEBI:57945; EC=1.1.1.23;
CC         Evidence={ECO:0000256|ARBA:ARBA00001654,
CC         ECO:0000256|PIRNR:PIRNR001257};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC       {ECO:0000256|ARBA:ARBA00005204}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC       {ECO:0000256|ARBA:ARBA00005169}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC       {ECO:0000256|ARBA:ARBA00004940}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the histidinol
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00008260,
CC       ECO:0000256|PIRNR:PIRNR001257}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KJR81359.1}.
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DR   EMBL; AXCR01000011; KJR81359.1; -; Genomic_DNA.
DR   RefSeq; XP_016584035.1; XM_016727952.1.
DR   AlphaFoldDB; A0A0F2LWX6; -.
DR   GeneID; 27663229; -.
DR   KEGG; ssck:SPSK_01021; -.
DR   VEuPathDB; FungiDB:SPSK_01021; -.
DR   OrthoDB; 50870at2759; -.
DR   UniPathway; UPA00031; UER00007.
DR   Proteomes; UP000033710; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06572; Histidinol_dh; 1.
DR   CDD; cd11546; NTP-PPase_His4; 1.
DR   Gene3D; 1.20.5.1300; -; 1.
DR   Gene3D; 1.10.287.1080; MazG-like; 1.
DR   Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2.
DR   Gene3D; 3.10.20.810; Phosphoribosyl-AMP cyclohydrolase; 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   NCBIfam; TIGR00069; hisD; 1.
DR   NCBIfam; TIGR03188; histidine_hisI; 1.
DR   PANTHER; PTHR21256:SF2; HISTIDINE BIOSYNTHESIS TRIFUNCTIONAL PROTEIN; 1.
DR   PANTHER; PTHR21256; HISTIDINOL DEHYDROGENASE HDH; 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   SUPFAM; SSF53720; ALDH-like; 1.
DR   SUPFAM; SSF101386; all-alpha NTP pyrophosphatases; 1.
DR   SUPFAM; SSF141734; HisI-like; 1.
DR   PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|PIRNR:PIRNR001257};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001257};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102,
KW   ECO:0000256|PIRNR:PIRNR001257};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001257};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NAD {ECO:0000256|PIRNR:PIRNR001257};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR001257};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR001257}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          234..305
FT                   /note="Phosphoribosyl-AMP cyclohydrolase"
FT                   /evidence="ECO:0000259|Pfam:PF01502"
SQ   SEQUENCE   873 AA;  91094 MW;  F9D6F602EC4F9F9D CRC64;
     MESTLPLPFV VSVPAALDSV SEGLTPAEIA VLGTIFLQAN PANLSQLQAL LAARGAELVP
     FVDGTALTSP DDVVALLDLG ARRVFVQPSQ LAELAPTYGA RVAAAVSATD ASAASLASAT
     TAEQGGLLVT DLDVAASTSS AFIEAAAATK TNPSLFVQPA PASVATPTAV STFAESAARI
     HAIPILPSTA LTTVTDSQDK VSVAGLLEAA WQSDRPDKLV TTVVTDQSGA ALGLVYSSVA
     SVAEALRTQT GVYQSRKRGL WHKGATSGDT QTLLRIGLDC DRDALHFVVR QEGRRFCHLD
     QFGCFGDLQG VARLDQTLRA RKASAPAGSY TARLFSDEKL LRAKIMEEAE ELCDAKTQQE
     VAFEAADLIY FALVKATAAG VSLADIERSL DAKGLKVQRR PGNAKPKWEE KVTEKAAAAP
     AAAVAVAKPS VDDRIAMKRI DASKVSAADI DEALRRPSQK SSEAIMKIVT PIIDDVRANG
     DKALLSYTHK FEKATSLTSP VLKAPFPPEL MQLSDETRAA IDLSFNNIRT FHAAQKEDKP
     LSVETMPGVV CSRFARPIAR VGLYVPGGTA VLPSTALMLG VPAMVAGCST IVLASPPRAD
     GTITPEIVYV AHKVGAESIV LAGGAQAVAA MAYGTESVSK VDKILGPGNQ FVTAAKMLVS
     NDTNAGVGID MPAGPSEVLV VADAEANPAF VASDLLSQAE HGVDSQVVLL AVDLSEAQLA
     AIEAEVHSQA MALPRVDIVR GAIGHSVTVQ VPNLDVAMAV SNAYAPEHLI LQVRDAPALV
     PKVLNAGSVF VGAWTPESVG DYSAGVNHSL PTYGFAKQYS GVNLGSFVKH ITSSNLTVEG
     LRNVGGAVMQ LAKVEELEAH RRAVSIRLAS LEK
//

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