HIS2_CANAX
ID HIS2_CANAX Reviewed; 838 AA.
AC O74712;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Histidine biosynthesis trifunctional protein;
DE Includes:
DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase;
DE EC=3.5.4.19;
DE Includes:
DE RecName: Full=Phosphoribosyl-ATP pyrophosphohydrolase;
DE EC=3.6.1.31;
DE Includes:
DE RecName: Full=Histidinol dehydrogenase;
DE Short=HDH;
DE EC=1.1.1.23;
GN Name=HIS4;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 64385 / 1001;
RX PubMed=9778800;
RX DOI=10.1002/(sici)1097-0061(19980915)14:12<1147::aid-yea297>3.0.co;2-7;
RA Navarro-Garcia F., Perez-Diaz R., Negredo A., Pla J., Nombela C.;
RT "Cloning and sequence of a 3.835 kbp DNA fragment containing the HIS4 gene
RT and a fragment of a PEX5-like gene from Candida albicans.";
RL Yeast 14:1147-1157(1998).
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 -!- 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 -!- 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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
CC -!- SIMILARITY: In the C-terminal section; belongs to the histidinol
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; AJ003115; CAA05871.1; -; Genomic_DNA.
DR AlphaFoldDB; O74712; -.
DR SMR; O74712; -.
DR VEuPathDB; FungiDB:C4_00140C_A; -.
DR VEuPathDB; FungiDB:CAWG_03769; -.
DR VEuPathDB; FungiDB:CAWG_03770; -.
DR UniPathway; UPA00031; UER00007.
DR UniPathway; UPA00031; UER00008.
DR UniPathway; UPA00031; UER00014.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd06572; Histidinol_dh; 1.
DR Gene3D; 3.10.20.810; -; 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 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;
KW Amino-acid biosynthesis; ATP-binding; Histidine biosynthesis; Hydrolase;
KW Metal-binding; Multifunctional enzyme; NAD; Nucleotide-binding;
KW Oxidoreductase; Zinc.
FT CHAIN 1..838
FT /note="Histidine biosynthesis trifunctional protein"
FT /id="PRO_0000135909"
FT REGION 1..271
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT REGION 272..360
FT /note="Phosphoribosyl-ATP pyrophosphohydrolase"
FT REGION 361..838
FT /note="Histidinol dehydrogenase"
FT ACT_SITE 729
FT /evidence="ECO:0000250"
FT ACT_SITE 730
FT /evidence="ECO:0000250"
FT BINDING 660
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 663
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 764
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 823
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 838 AA; 91836 MW; BFA0E97E9CA62C03 CRC64;
MIFPILPVIS SPEDKQSIDE FSLVGQVLFP IESVSPKKHF IHQFPHDLDI FVNAIDNATT
DQIVELLNVG IKQVFVNEKQ YHDAIEAGSP SSRFVVAVDV PSTELLTSEA SFVTSKPFSE
SDLKKYNANE NRVIYIESNF TQDGAIELAK NYVPVIPSTK LTVKREEENK ISISAVFVST
LTTDRPDGLY TTLITTPSPS YTALGIVYSS KDSIIAAIEE KVGVYQSRKR RDELWYKGKT
SGATQKLVKL SKDCDSDVIQ FMVEPRTGYG FCHRETKFTC FGDDIADSPA RGLPKLDSTL
QDRLENAPEG SYTKRLFDDE KLLIAKLKEE LDELIEAKSK EEIAWECADL VYFAMVWCIK
HGVRLADIEK NLDVKSLKVS RRKGDAKPQY QEAPVNSSYK LEIVSVDDAA AVERAMTRPV
QKTADIMKLV LPIIEKVKSD GDKALIELTS KFDGVKLDAP VLQAPFPADL MDISEEMKAA
IDLSMQNIEK FHAAQLPKEK VMTVETSPGV YCSRFAKPIE NVGLYVPGGT AVLPSTAMML
GVPAKVAGCK NIIVASPPSR ATGKLTPEVV YVAHKLGAKC IVMAGGAQAV TAMAYGTESV
LKCDKILGPG NQFVTAAKMY VQNDTQALCS IDMPAGPSEV LVIADSNADA DFVASDLLSQ
AEHGVDSQVI LIGVGLSDEK LNEFQAAVER QAKVLPRKDI VAKCLAHSYI LLAKTYKEAF
DLSNQYAPEH LILQIDDAPS YVPDSIENAG SVFVGALSPE SCGDYSSGTN HTLPTYGYAR
QYSGVNTATF QKFITSQEVT EKGLQNIGKA VMELARVEGL EAHRRAVEIR MERMAETK
