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O13471 (HIS2_KLULA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 105. 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
Ordered Locus Names:KLLA0C01452g
OrganismKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]
Taxonomic identifier284590 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces

Protein attributes

Sequence length795 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 – 795795Histidine biosynthesis trifunctional protein HAMAP-Rule MF_01024
PRO_0000135910

Regions

Region1 – 225225Phosphoribosyl-AMP cyclohydrolase HAMAP-Rule MF_01024
Region226 – 30883Phosphoribosyl-ATP pyrophosphohydrolase HAMAP-Rule MF_01024
Region309 – 795487Histidinol dehydrogenase HAMAP-Rule MF_01024

Sites

Active site6831 By similarity
Active site6841 By similarity
Metal binding6141Zinc By similarity
Metal binding6171Zinc By similarity
Metal binding7171Zinc By similarity
Metal binding7761Zinc By similarity

Experimental info

Sequence conflict162 – 1632VY → DI in CAA70698. Ref.1
Sequence conflict580 – 5823QAL → LAI in CAA70698. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O13471 [UniParc].

Last modified September 27, 2004. Version 2.
Checksum: 6D35F1632280D3B3

FASTA79586,795
        10         20         30         40         50         60 
MLPVVPVFNA VNALKEKTYL YLSSQLVLDG KDMTKDDILE FVQNSHGQNI SVLLKDAKFE 

        70         80         90        100        110        120 
DDDLIVLLNN GVVTLFIDSD DYAAHLVEIG VPSIRLTLLK DGAYQFSFGQ IQEIQQSQLV 

       130        140        150        160        170        180 
KASEISLETF TNSVLSGMKT DRPDGLYTTL VVDENERSLG LVYSNKESVS LAIETQTGIY 

       190        200        210        220        230        240 
FSRSRNEIWR KGATSGNVQK LLSIELDCDG DALKFVVRQG GSGSFCHLET ESCFGNFRHG 

       250        260        270        280        290        300 
LYGLQKLLQE RLLNAPEGSY TKRLFNDSDL LTAKIKEEAE ELTEAVDKKD IAWECADLFY 

       310        320        330        340        350        360 
FAMARLVANG VSLEDVERNL NTKHLKITRR KGDAKPKFLK KEPVAVHEED GKIVLNVVSA 

       370        380        390        400        410        420 
SDKAAVEKAV TRPIQKTAEI MNLVNPIIEN VIKNGDKALV ELTAKFDGVQ LETPVLEAPY 

       430        440        450        460        470        480 
PEEYLDGLTD ELRDALDLSI ENVKKFHAAQ MQSETLDVET QPGVVCSRFP RPIEKVGLYI 

       490        500        510        520        530        540 
PGGTAILPST ALMLGVPAQV AGCKEIVFAS PPRKSDGRVS PEVVYVASKV GASKIVLAGG 

       550        560        570        580        590        600 
AQAIAAMAYG TESVPKVDKI LGPGNQFVTA AKMYVQNDTQ ALCSIDMPAG PSEVLVICDE 

       610        620        630        640        650        660 
EADVDFVASD LLSQAEHGID SQVILVGVSL SDSKIEALQN AVHEQAMQLP RVDIVRKCIA 

       670        680        690        700        710        720 
HSSIILCDSY EEAFKMSNQY APEHLILQIS NAEDYVKDVD HAGSIFVGAY TPESCGDYSS 

       730        740        750        760        770        780 
GTNHTLPTYG YARQYSGVNT ATFQKFITSQ VVTPVGLEHI GHAVMSVAKV EGLDAHRNAV 

       790 
KIRMSKLGLL PSGFE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y09503 Genomic DNA. Translation: CAA70698.1.
CR382123 Genomic DNA. Translation: CAH01111.1.
RefSeqXP_452260.1. XM_452260.1.

3D structure databases

ProteinModelPortalO13471.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING28985.O13471.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2892606.
KEGGkla:KLLA0C01452g.

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK14152.
OMANIRKFHA.
OrthoDBEOG7DJSVM.

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_KLULA
AccessionPrimary (citable) accession number: O13471
Secondary accession number(s): Q6CUX9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: September 27, 2004
Last modified: February 19, 2014
This is version 105 of the entry and version 2 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