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Protein

Histidine biosynthesis trifunctional protein

Gene

HIS4

Organism
Saccharomyces bayanus (Yeast) (Saccharomyces uvarum x Saccharomyces eubayanus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

1-(5-phospho-beta-D-ribosyl)-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D-ribosylamino)methylideneamino)imidazole-4-carboxamide.
1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-AMP + diphosphate.
L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi618 – 6181ZincBy similarity
Metal bindingi621 – 6211ZincBy similarity
Active sitei687 – 6871By similarity
Active sitei688 – 6881By similarity
Metal bindingi721 – 7211ZincBy similarity
Metal bindingi780 – 7801ZincBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. histidinol dehydrogenase activity Source: UniProtKB-EC
  3. NAD binding Source: InterPro
  4. phosphoribosyl-AMP cyclohydrolase activity Source: UniProtKB-EC
  5. phosphoribosyl-ATP diphosphatase activity Source: UniProtKB-EC
  6. zinc ion binding Source: InterPro

GO - Biological processi

  1. histidine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, NAD, Nucleotide-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00031; UER00007.
UPA00031; UER00008.
UPA00031; UER00014.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidine biosynthesis trifunctional protein
Including the following 3 domains:
Phosphoribosyl-AMP cyclohydrolase (EC:3.5.4.19)
Phosphoribosyl-ATP pyrophosphohydrolase (EC:3.6.1.31)
Histidinol dehydrogenase (EC:1.1.1.23)
Short name:
HDH
Gene namesi
Name:HIS4
OrganismiSaccharomyces bayanus (Yeast) (Saccharomyces uvarum x Saccharomyces eubayanus)
Taxonomic identifieri4931 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 799799Histidine biosynthesis trifunctional proteinPRO_0000135913Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ12670.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 229229Phosphoribosyl-AMP cyclohydrolaseAdd
BLAST
Regioni230 – 31283Phosphoribosyl-ATP pyrophosphohydrolaseAdd
BLAST
Regioni313 – 799487Histidinol dehydrogenaseAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the histidinol dehydrogenase family.Curated

Family and domain databases

HAMAPiMF_01024. HisD.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016298. Histidine_synth_trifunct.
IPR001692. Histidinol_DH_CS.
IPR012131. Hstdl_DH.
IPR008179. PRib-ATP_PPHydrolase.
IPR021130. PRib-ATP_PPHydrolase-like.
IPR002496. PRib_AMP_CycHydrolase_dom.
[Graphical view]
PfamiPF00815. Histidinol_dh. 1 hit.
PF01502. PRA-CH. 1 hit.
PF01503. PRA-PH. 1 hit.
[Graphical view]
PIRSFiPIRSF001257. His_trifunctional. 1 hit.
PRINTSiPR00083. HOLDHDRGNASE.
ProDomiPD002610. PRA_CycHdrlase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
TIGR03188. histidine_hisI. 1 hit.
PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12670-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLPILPLID DLASWGTKKA YASLVGQVLL DGSSLNKDEV LQFAKEEEVP
60 70 80 90 100
LVALSLPNAK FSDDDIIAFL NNGVSSLFIA SQDAKIVDHL VEELNVPKNR
110 120 130 140 150
IVVEGNGVFH NQFLVNQKFS QDRIVSIKKL TKDLLIKEVV AEVRTDRPDG
160 170 180 190 200
LFTTLVVDQY ERCLGLVYSS KESIAKAIDL GRGVYYSRSR NEIWVKGETS
210 220 230 240 250
GNGQKLLQIS TDCDSDALKF IVEQENVGFC HLETMSCFGE FKHGLVGLES
260 270 280 290 300
LLKQRLQDAP KESYTRRLFN DPALLDAKIK EEAEELTEAK GKQEISWEAA
310 320 330 340 350
DLFYFALAKL VTNNVSLKDV ENNLNMKHLK ITRRKGDAKP KFVAQAKAEE
360 370 380 390 400
EAPTGPIHLH VVNASDKEGI KKALSRPIQK TSEIMHLVNP IIENVRDRGD
410 420 430 440 450
SALLEYTEKF DGVKLSTPVL NAPFPEEYFE GLTEEMKDAL DLSIENVRKF
460 470 480 490 500
HAAQLPKETL EVETQPGVLC SRFPRPIEKV GLYIPGGTAI LPSTALMLGV
510 520 530 540 550
PAQVAQCKEI VFASPPRKSD GKVSPEVVYV AEKVGARMIV LAGGAQAVAA
560 570 580 590 600
MAYGTETIPK VDKVLGPGNQ FVTAAKMYVQ NDTQALCSID MPAGPSEVLV
610 620 630 640 650
IADEDADADF VASDLLSQAE HGIDSQVILV GIKLSEKKIQ EIQDAVHDQA
660 670 680 690 700
MQLPRVDIVR KCIAHSTIIL CDGYEEALEM SNKYAPEHLI LQIANANDYV
710 720 730 740 750
KLVDNAGSVF VGAYTPESCG DYSSGTNHTL PTYGYARQYS GANTATFQKF
760 770 780 790
ITAQNITPEG LENIGRAVMC VAKKEGLDGH RNAVKIRMSK LGLIPKDFQ
Length:799
Mass (Da):87,734
Last modified:November 1, 1996 - v1
Checksum:i35793E26EDB81B6B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13062 Genomic DNA. Translation: AAA21153.1.
AJ251575 Genomic DNA. Translation: CAC16411.1.
PIRiS53349.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13062 Genomic DNA. Translation: AAA21153.1.
AJ251575 Genomic DNA. Translation: CAC16411.1.
PIRiS53349.

3D structure databases

ProteinModelPortaliQ12670.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00031; UER00007.
UPA00031; UER00008.
UPA00031; UER00014.

Family and domain databases

HAMAPiMF_01024. HisD.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016298. Histidine_synth_trifunct.
IPR001692. Histidinol_DH_CS.
IPR012131. Hstdl_DH.
IPR008179. PRib-ATP_PPHydrolase.
IPR021130. PRib-ATP_PPHydrolase-like.
IPR002496. PRib_AMP_CycHydrolase_dom.
[Graphical view]
PfamiPF00815. Histidinol_dh. 1 hit.
PF01502. PRA-CH. 1 hit.
PF01503. PRA-PH. 1 hit.
[Graphical view]
PIRSFiPIRSF001257. His_trifunctional. 1 hit.
PRINTSiPR00083. HOLDHDRGNASE.
ProDomiPD002610. PRA_CycHdrlase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
TIGR03188. histidine_hisI. 1 hit.
PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The polyfunctional HIS4 gene of Saccharomyces carlsbergensis: sequence and homology analysis."
    Porter G.L.
    Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Analysis of the constitution of the beer yeast genome by PCR, sequencing and subtelomeric sequence hybridization."
    Casaregola S., Nguyen H.V., Lapathitis G., Kotyk A., Gaillardin C.
    Int. J. Syst. Evol. Microbiol. 51:1607-1618(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53.
    Strain: ATCC 76513 / CBS 380 / DSM 70412 / JCM 7258 / NBRC 1127 / NRRL Y-12624.

Entry informationi

Entry nameiHIS2_SACBA
AccessioniPrimary (citable) accession number: Q12670
Secondary accession number(s): Q9HFG2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.