Histidine biosynthesis trifunctional protein - Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast)

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O13471 (HIS2_KLULA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 102. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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
Short name=HDH
EC=1.1.1.23

Gene names

Name:	HIS4
Ordered Locus Names:	KLLA0C01452g

Organism

Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

284590 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces ›

Protein attributes

Sequence length	795 AA.
Sequence status	Complete.
Protein existence	Inferred 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. 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.
Cofactor	Binds 1 zinc ion By similarity.
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. 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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Ligand	ATP-binding Metal-binding NAD Nucleotide-binding Zinc
Molecular function	Hydrolase Oxidoreductase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological_process	histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW NAD binding Inferred from electronic annotation. Source: InterPro histidinol dehydrogenase activity Inferred from electronic annotation. Source: EC phosphoribosyl-AMP cyclohydrolase activity Inferred from electronic annotation. Source: EC phosphoribosyl-ATP diphosphatase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 795

795

Histidine biosynthesis trifunctional protein

PRO_0000135910

Regions

Region

1 – 225

225

Phosphoribosyl-AMP cyclohydrolase

Region

226 – 308

Phosphoribosyl-ATP pyrophosphohydrolase

Region

309 – 795

487

Histidinol dehydrogenase

Sites

Active site

683

By similarity

Active site

684

By similarity

Metal binding

614

Zinc By similarity

Metal binding

617

Zinc By similarity

Metal binding

717

Zinc By similarity

Metal binding

776

Zinc By similarity

Experimental info

Sequence conflict

162 – 163

VY → DI in CAA70698. Ref.1

Sequence conflict

580 – 582

QAL → LAI in CAA70698. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

O13471 [UniParc].

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

FASTA

795

86,795

        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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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. 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y09503 Genomic DNA. Translation: CAA70698.1. CR382123 Genomic DNA. Translation: CAH01111.1.
RefSeq	XP_452260.1. XM_452260.1.
3D structure databases
ProteinModelPortal	O13471.
ModBase	Search...
Protein-protein interaction databases
STRING	28985.O13471.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2892606.
KEGG	kla:KLLA0C01452g.
Phylogenomic databases
eggNOG	COG0141.
HOGENOM	HOG000243914.
KO	K14152.
OMA	LGPGNQF.
OrthoDB	EOG44N216.
Enzyme and pathway databases
UniPathway	UPA00031; UER00007. UPA00031; UER00008. UPA00031; UER00014.
Family and domain databases
InterPro	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]
Pfam	PF00815. Histidinol_dh. 1 hit. PF01502. PRA-CH. 1 hit. PF01503. PRA-PH. 1 hit. [Graphical view]
PIRSF	PIRSF001257. His_trifunctional. 1 hit.
PRINTS	PR00083. HOLDHDRGNASE.
ProDom	PD002610. PRA_CycHdrlase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SUPFAM	SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMs	TIGR00069. hisD. 1 hit. TIGR03188. histidine_hisI. 1 hit.
PROSITE	PS00611. HISOL_DEHYDROGENASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HIS2_KLULA

Accession

Primary (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:	May 29, 2013
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 3 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents