UniProt: C1H3R3

Database: UniProt
Entry: C1H3R3_PARBA

LinkDB:  C1H3R3_PARBA 
Original site:  C1H3R3_PARBA

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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 (1)   
   PubMed (1)   
All databases (27)   

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ID   C1H3R3_PARBA            Unreviewed;       870 AA.
AC   C1H3R3;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   13-SEP-2023, entry version 74.
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=PAAG_05406 {ECO:0000313|EMBL:EEH34357.1};
OS   Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS   brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH34357.1, ECO:0000313|Proteomes:UP000002059};
RN   [1] {ECO:0000313|EMBL:EEH34357.1, ECO:0000313|Proteomes:UP000002059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
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}.
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DR   EMBL; KN294005; EEH34357.1; -; Genomic_DNA.
DR   RefSeq; XP_002792677.1; XM_002792631.1.
DR   AlphaFoldDB; C1H3R3; -.
DR   STRING; 502779.C1H3R3; -.
DR   GeneID; 9096031; -.
DR   KEGG; pbl:PAAG_05406; -.
DR   VEuPathDB; FungiDB:PAAG_05406; -.
DR   eggNOG; KOG2697; Eukaryota.
DR   eggNOG; KOG4311; Eukaryota.
DR   HOGENOM; CLU_006732_0_0_1; -.
DR   OMA; VFVVKQI; -.
DR   OrthoDB; 50870at2759; -.
DR   UniPathway; UPA00031; UER00007.
DR   Proteomes; UP000002059; Partially assembled 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002059};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          226..297
FT                   /note="Phosphoribosyl-AMP cyclohydrolase"
FT                   /evidence="ECO:0000259|Pfam:PF01502"
SQ   SEQUENCE   870 AA;  93098 MW;  E5B2B713C83A064B CRC64;
     MGIPFLVSVD PQTLSSTSPA AHLTIKQISY FGRVLLKSSS LSQVISFVKQ FSSLLDIYAD
     ATTIDSAGDV LDILNSGASK VLVTPTQLTT LTGEQAVPSS RLIISVSSAI GAGGLQSWIA
     EDDERKNIGL HCVVSSVVDD VVEELVERGF VKEVYLSYDG AEAVTKAALN SSQKENVVTV
     IPSIALSLDN GDASPAKLLV AGATADQTTG LYTTVVTDER GVALGLVYSS EHSISEALKT
     GTGVYQSRKR GLWHKGQSSG DTQELVRVDF DCDSDCLLFV VKQKGRGFCH LGTASCFGQY
     RGLSRLQKTL QSRKENAPPG SYTARLFNDP KFVQAKIMEE AEELCNAKSK EEVAFEAADL
     LYFALTRCIA AGVSLEDVER NLDLKSLQVK RRQGDAKQGW AKKVGLESTK EEQKNKVEPT
     NANDVNRKIE MRRVVTATAS QDTLEEALKR PSQKSNDAIV ALVKPIIEDI RKNGDAAVLK
     YTHKFEKATS LTSPVIKAPF PANLMQVTPE TANAINISFE NIRNFHAAQK DDKPLHVETM
     PGVVCSRFSR VIERVGLYVP GGTAVLPSTA MMLGVPAMVA GCKKIVLASP PRSDGSISPE
     IVYIAHKVGA ESIVLAGGAQ AVAAMAYGTE SISKVDKILG PGNQFVTAAK MLVSNDTSAG
     VSIDMPAGPS EVLVVADKNA NPAFVASDLL SQAEHGVDSQ VILVAVDLDD SHLKAIEEEL
     HAQAMALPRV DIVRGAIDHS VTFVVKDIDE AIALSNRYAP EHLILQVKNA ADVVPLVQNA
     GSVFIGEWTP ESVGDYSAGV NHSLPTYGYA KQYSGVNLAS FVKHITSSNL TAEGLRNVGG
     AVMELASVEG LDAHRRAVSI RLDHMDRSRK
//

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