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Q12670 (HIS2_SACBA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histidine biosynthesis trifunctional protein

Including the following 3 domains:

  1. Phosphoribosyl-AMP cyclohydrolase
    EC=3.5.4.19
  2. Phosphoribosyl-ATP pyrophosphohydrolase
    EC=3.6.1.31
  3. Histidinol dehydrogenase
    Short name=HDH
    EC=1.1.1.23
Gene names
Name:HIS4
OrganismSaccharomyces bayanus (Yeast) (Saccharomyces uvarum x Saccharomyces eubayanus)
Taxonomic identifier4931 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length799 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

1-(5-phospho-beta-D-ribosyl)-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D-ribosylamino)methylideneamino)imidazole-4-carboxamide. HAMAP-Rule MF_01024

1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-AMP + diphosphate. HAMAP-Rule MF_01024

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. HAMAP-Rule MF_01024

Cofactor

Binds 1 zinc ion By similarity. HAMAP-Rule MF_01024

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. HAMAP-Rule MF_01024

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 799799Histidine biosynthesis trifunctional protein HAMAP-Rule MF_01024
PRO_0000135913

Regions

Region1 – 229229Phosphoribosyl-AMP cyclohydrolase HAMAP-Rule MF_01024
Region230 – 31283Phosphoribosyl-ATP pyrophosphohydrolase HAMAP-Rule MF_01024
Region313 – 799487Histidinol dehydrogenase HAMAP-Rule MF_01024

Sites

Active site6871 By similarity
Active site6881 By similarity
Metal binding6181Zinc By similarity
Metal binding6211Zinc By similarity
Metal binding7211Zinc By similarity
Metal binding7801Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q12670 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 35793E26EDB81B6B

FASTA79987,734
        10         20         30         40         50         60 
MVLPILPLID DLASWGTKKA YASLVGQVLL DGSSLNKDEV LQFAKEEEVP LVALSLPNAK 

        70         80         90        100        110        120 
FSDDDIIAFL NNGVSSLFIA SQDAKIVDHL VEELNVPKNR IVVEGNGVFH NQFLVNQKFS 

       130        140        150        160        170        180 
QDRIVSIKKL TKDLLIKEVV AEVRTDRPDG LFTTLVVDQY ERCLGLVYSS KESIAKAIDL 

       190        200        210        220        230        240 
GRGVYYSRSR NEIWVKGETS GNGQKLLQIS TDCDSDALKF IVEQENVGFC HLETMSCFGE 

       250        260        270        280        290        300 
FKHGLVGLES LLKQRLQDAP KESYTRRLFN DPALLDAKIK EEAEELTEAK GKQEISWEAA 

       310        320        330        340        350        360 
DLFYFALAKL VTNNVSLKDV ENNLNMKHLK ITRRKGDAKP KFVAQAKAEE EAPTGPIHLH 

       370        380        390        400        410        420 
VVNASDKEGI KKALSRPIQK TSEIMHLVNP IIENVRDRGD SALLEYTEKF DGVKLSTPVL 

       430        440        450        460        470        480 
NAPFPEEYFE GLTEEMKDAL DLSIENVRKF HAAQLPKETL EVETQPGVLC SRFPRPIEKV 

       490        500        510        520        530        540 
GLYIPGGTAI LPSTALMLGV PAQVAQCKEI VFASPPRKSD GKVSPEVVYV AEKVGARMIV 

       550        560        570        580        590        600 
LAGGAQAVAA MAYGTETIPK VDKVLGPGNQ FVTAAKMYVQ NDTQALCSID MPAGPSEVLV 

       610        620        630        640        650        660 
IADEDADADF VASDLLSQAE HGIDSQVILV GIKLSEKKIQ EIQDAVHDQA MQLPRVDIVR 

       670        680        690        700        710        720 
KCIAHSTIIL CDGYEEALEM SNKYAPEHLI LQIANANDYV KLVDNAGSVF VGAYTPESCG 

       730        740        750        760        770        780 
DYSSGTNHTL PTYGYARQYS GANTATFQKF ITAQNITPEG LENIGRAVMC VAKKEGLDGH 

       790 
RNAVKIRMSK LGLIPKDFQ 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U13062 Genomic DNA. Translation: AAA21153.1.
AJ251575 Genomic DNA. Translation: CAC16411.1.
PIRS53349.

3D structure databases

ProteinModelPortalQ12670.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00031; UER00007.
UPA00031; UER00008.
UPA00031; UER00014.

Family and domain databases

HAMAPMF_01024. HisD.
InterProIPR016161. 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]
PfamPF00815. Histidinol_dh. 1 hit.
PF01502. PRA-CH. 1 hit.
PF01503. PRA-PH. 1 hit.
[Graphical view]
PIRSFPIRSF001257. His_trifunctional. 1 hit.
PRINTSPR00083. HOLDHDRGNASE.
ProDomPD002610. PRA_CycHdrlase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR00069. hisD. 1 hit.
TIGR03188. histidine_hisI. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHIS2_SACBA
AccessionPrimary (citable) accession number: Q12670
Secondary accession number(s): Q9HFG2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways