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O13471

- HIS2_KLULA

UniProt

O13471 - HIS2_KLULA

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Protein

Histidine biosynthesis trifunctional protein

Gene
HIS4, KLLA0C01452g
Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed - 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.UniRule annotation
1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-AMP + diphosphate.UniRule annotation
L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.UniRule annotation

Cofactori

Binds 1 zinc ion By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi614 – 6141Zinc By similarity
Metal bindingi617 – 6171Zinc By similarity
Active sitei683 – 6831 By similarity
Active sitei684 – 6841 By similarity
Metal bindingi717 – 7171Zinc By similarity
Metal bindingi776 – 7761Zinc By 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
Ordered Locus Names:KLLA0C01452g
OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic identifieri284590 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
ProteomesiUP000000598: Chromosome C

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 795795Histidine biosynthesis trifunctional proteinUniRule annotationPRO_0000135910Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi28985.O13471.

Structurei

3D structure databases

ProteinModelPortaliO13471.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 225225Phosphoribosyl-AMP cyclohydrolaseUniRule annotationAdd
BLAST
Regioni226 – 30883Phosphoribosyl-ATP pyrophosphohydrolaseUniRule annotationAdd
BLAST
Regioni309 – 795487Histidinol dehydrogenaseUniRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK14152.
OMAiNIRKFHA.
OrthoDBiEOG7DJSVM.

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.

O13471-1 [UniParc]FASTAAdd to Basket

« Hide

MLPVVPVFNA VNALKEKTYL YLSSQLVLDG KDMTKDDILE FVQNSHGQNI    50
SVLLKDAKFE DDDLIVLLNN GVVTLFIDSD DYAAHLVEIG VPSIRLTLLK 100
DGAYQFSFGQ IQEIQQSQLV KASEISLETF TNSVLSGMKT DRPDGLYTTL 150
VVDENERSLG LVYSNKESVS LAIETQTGIY FSRSRNEIWR KGATSGNVQK 200
LLSIELDCDG DALKFVVRQG GSGSFCHLET ESCFGNFRHG LYGLQKLLQE 250
RLLNAPEGSY TKRLFNDSDL LTAKIKEEAE ELTEAVDKKD IAWECADLFY 300
FAMARLVANG VSLEDVERNL NTKHLKITRR KGDAKPKFLK KEPVAVHEED 350
GKIVLNVVSA SDKAAVEKAV TRPIQKTAEI MNLVNPIIEN VIKNGDKALV 400
ELTAKFDGVQ LETPVLEAPY PEEYLDGLTD ELRDALDLSI ENVKKFHAAQ 450
MQSETLDVET QPGVVCSRFP RPIEKVGLYI PGGTAILPST ALMLGVPAQV 500
AGCKEIVFAS PPRKSDGRVS PEVVYVASKV GASKIVLAGG AQAIAAMAYG 550
TESVPKVDKI LGPGNQFVTA AKMYVQNDTQ ALCSIDMPAG PSEVLVICDE 600
EADVDFVASD LLSQAEHGID SQVILVGVSL SDSKIEALQN AVHEQAMQLP 650
RVDIVRKCIA HSSIILCDSY EEAFKMSNQY APEHLILQIS NAEDYVKDVD 700
HAGSIFVGAY TPESCGDYSS GTNHTLPTYG YARQYSGVNT ATFQKFITSQ 750
VVTPVGLEHI GHAVMSVAKV EGLDAHRNAV KIRMSKLGLL PSGFE 795
Length:795
Mass (Da):86,795
Last modified:September 27, 2004 - v2
Checksum:i6D35F1632280D3B3
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti162 – 1632VY → DI in CAA70698. 1 Publication
Sequence conflicti580 – 5823QAL → LAI in CAA70698. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y09503 Genomic DNA. Translation: CAA70698.1.
CR382123 Genomic DNA. Translation: CAH01111.1.
RefSeqiXP_452260.1. XM_452260.1.

Genome annotation databases

GeneIDi2892606.
KEGGikla:KLLA0C01452g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y09503 Genomic DNA. Translation: CAA70698.1 .
CR382123 Genomic DNA. Translation: CAH01111.1 .
RefSeqi XP_452260.1. XM_452260.1.

3D structure databases

ProteinModelPortali O13471.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 28985.O13471.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2892606.
KEGGi kla:KLLA0C01452g.

Phylogenomic databases

eggNOGi COG0141.
HOGENOMi HOG000243914.
KOi K14152.
OMAi NIRKFHA.
OrthoDBi EOG7DJSVM.

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00007 .
UPA00031 ; UER00008 .
UPA00031 ; UER00014 .

Family and domain databases

HAMAPi MF_01024. HisD.
InterProi IPR016161. 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 ]
Pfami PF00815. Histidinol_dh. 1 hit.
PF01502. PRA-CH. 1 hit.
PF01503. PRA-PH. 1 hit.
[Graphical view ]
PIRSFi PIRSF001257. His_trifunctional. 1 hit.
PRINTSi PR00083. HOLDHDRGNASE.
ProDomi PD002610. PRA_CycHdrlase. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF53720. SSF53720. 1 hit.
TIGRFAMsi TIGR00069. hisD. 1 hit.
TIGR03188. histidine_hisI. 1 hit.
PROSITEi PS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The HIS4 gene from the yeast Kluyveromyces lactis."
    Freire-Picos M.A., Hampsey M., Cerdan M.E.
    Yeast 14:687-691(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.
  2. "Genome evolution in yeasts."
    Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.
    , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
    Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

Entry informationi

Entry nameiHIS2_KLULA
AccessioniPrimary (citable) accession number: O13471
Secondary accession number(s): Q6CUX9
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

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