HIS2_SACBA
ID HIS2_SACBA Reviewed; 799 AA.
AC Q12670; Q9HFG2;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 110.
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 Saccharomyces bayanus (Yeast) (Saccharomyces uvarum x Saccharomyces
OS eubayanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=4931;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Porter G.L.;
RT "The polyfunctional HIS4 gene of Saccharomyces carlsbergensis: sequence and
RT homology analysis.";
RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53.
RC STRAIN=ATCC 76513 / CBS 380 / DSM 70412 / JCM 7258 / NBRC 1127 / NRRL
RC Y-12624;
RX PubMed=11491364; DOI=10.1099/00207713-51-4-1607;
RA Casaregola S., Nguyen H.V., Lapathitis G., Kotyk A., Gaillardin C.;
RT "Analysis of the constitution of the beer yeast genome by PCR, sequencing
RT and subtelomeric sequence hybridization.";
RL Int. J. Syst. Evol. Microbiol. 51:1607-1618(2001).
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; U13062; AAA21153.1; -; Genomic_DNA.
DR EMBL; AJ251575; CAC16411.1; -; Genomic_DNA.
DR PIR; S53349; S53349.
DR AlphaFoldDB; Q12670; -.
DR SMR; Q12670; -.
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..799
FT /note="Histidine biosynthesis trifunctional protein"
FT /id="PRO_0000135913"
FT REGION 1..229
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT REGION 230..312
FT /note="Phosphoribosyl-ATP pyrophosphohydrolase"
FT REGION 313..799
FT /note="Histidinol dehydrogenase"
FT ACT_SITE 687
FT /evidence="ECO:0000250"
FT ACT_SITE 688
FT /evidence="ECO:0000250"
FT BINDING 618
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 621
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 721
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 780
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 799 AA; 87734 MW; 35793E26EDB81B6B CRC64;
MVLPILPLID DLASWGTKKA YASLVGQVLL DGSSLNKDEV LQFAKEEEVP LVALSLPNAK
FSDDDIIAFL NNGVSSLFIA SQDAKIVDHL VEELNVPKNR IVVEGNGVFH NQFLVNQKFS
QDRIVSIKKL TKDLLIKEVV AEVRTDRPDG LFTTLVVDQY ERCLGLVYSS KESIAKAIDL
GRGVYYSRSR NEIWVKGETS GNGQKLLQIS TDCDSDALKF IVEQENVGFC HLETMSCFGE
FKHGLVGLES LLKQRLQDAP KESYTRRLFN DPALLDAKIK EEAEELTEAK GKQEISWEAA
DLFYFALAKL VTNNVSLKDV ENNLNMKHLK ITRRKGDAKP KFVAQAKAEE EAPTGPIHLH
VVNASDKEGI KKALSRPIQK TSEIMHLVNP IIENVRDRGD SALLEYTEKF DGVKLSTPVL
NAPFPEEYFE GLTEEMKDAL DLSIENVRKF HAAQLPKETL EVETQPGVLC SRFPRPIEKV
GLYIPGGTAI LPSTALMLGV PAQVAQCKEI VFASPPRKSD GKVSPEVVYV AEKVGARMIV
LAGGAQAVAA MAYGTETIPK VDKVLGPGNQ FVTAAKMYVQ NDTQALCSID MPAGPSEVLV
IADEDADADF VASDLLSQAE HGIDSQVILV GIKLSEKKIQ EIQDAVHDQA MQLPRVDIVR
KCIAHSTIIL CDGYEEALEM SNKYAPEHLI LQIANANDYV KLVDNAGSVF VGAYTPESCG
DYSSGTNHTL PTYGYARQYS GANTATFQKF ITAQNITPEG LENIGRAVMC VAKKEGLDGH
RNAVKIRMSK LGLIPKDFQ
