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P45353 (HIS2_PICPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 91. 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
OrganismKomagataella pastoris (Yeast) (Pichia pastoris)
Taxonomic identifier4922 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKomagataella

Protein attributes

Sequence length842 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 – 842842Histidine biosynthesis trifunctional protein HAMAP-Rule MF_01024
PRO_0000135912

Regions

Region1 – 275275Phosphoribosyl-AMP cyclohydrolase HAMAP-Rule MF_01024
Region276 – 35782Phosphoribosyl-ATP pyrophosphohydrolase HAMAP-Rule MF_01024
Region358 – 842485Histidinol dehydrogenase HAMAP-Rule MF_01024

Sites

Active site7361 By similarity
Active site7371 By similarity
Metal binding6671Zinc By similarity
Metal binding6701Zinc By similarity
Metal binding7691Zinc By similarity
Metal binding8281Zinc By similarity

Experimental info

Sequence conflict921R → RM Ref.2
Sequence conflict5071A → T in CAA39641. Ref.2
Sequence conflict6611V → A in CAA39641. Ref.2
Sequence conflict7461S → SS in CAA39641. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P45353 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 67DA24E2266A4A3E

FASTA84291,942
        10         20         30         40         50         60 
MTFPLLPAYA SVAEFDNSLS LVGKAVFPYA ADQLHNLIKF TQSTELQVNV QVESSVTEDQ 

        70         80         90        100        110        120 
FEELIDNLLK LYNNGINEVI LDLDLAERVV QRIPGARVIY RTLVDKVASL PANASIAVPF 

       130        140        150        160        170        180 
SSPLGDLKSF TNGGSRTVYA FSETAKLVDV TSTVASGIIP IIDARQLTTE YELSEDVKKF 

       190        200        210        220        230        240 
PVSEILLASL TTDRPDGLFT TLVADSSNYS LGLVYSSKKS IPEAIRTQTG VYQSRRHGLW 

       250        260        270        280        290        300 
YKGATSGATQ KLLGIELDCD GDCLKFVVEQ TGVGFCHLER TSCFGQSKGL RAMEATLWDR 

       310        320        330        340        350        360 
KSNAPEGSYT KRLFDDEVLL NAKIREEADE LAEAKSKEDI AWECADLFYF ALVRCAKYGV 

       370        380        390        400        410        420 
TLDEVERNLD MKSLKVTRRK GDAKPGYTKE QPKEESKPKE VPSEGRIELC KIDVSKASSQ 

       430        440        450        460        470        480 
EIEDALRRPI QKTEQIMELV KPIVDNVRQN GDKALLELTA KFDGVALKTP VLEAPFPEEL 

       490        500        510        520        530        540 
MQLPDNVKRA IDLSIDNVRK FHEAQLAETL QVETCPGVVC SRFARPIEKV GLYIPGGTAI 

       550        560        570        580        590        600 
LPSTSLMLGV PAKVAGCKEI VFASPPKKDG TLTPEVIYVA HKVGAKCIVL AGGAQAVAAM 

       610        620        630        640        650        660 
AYGTETVPKC DKIFGPGNQF VTAAKMMVQN DTSALCSIDM PAGPSEVLVI ADKYADPDFV 

       670        680        690        700        710        720 
VSDLLSQAEH GIDSQVILLA VDMTDKELAR IEDAVHNQAV QLPRVEIVRK CIAHSTTLSV 

       730        740        750        760        770        780 
ATYEQALEMS NQYAPEHLIL QIENASYVDQ VQHAGSVFVG AYSPESCGDY SSGTNHTLPT 

       790        800        810        820        830        840 
YGYARQYSGV NTATFQKFIT SQDVTPEGLK HIGQAVMDLA AVEGLDAHRN AVKVRMEKLG 


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References

[1]"The Pichia pastoris HIS4 gene: nucleotide sequence, creation of a non-reverting his4 deletion mutant, and development of HIS4-based replicating and integrating plasmids."
Crane D.I., Gould S.J.
Curr. Genet. 26:443-450(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Koutz P.J., Davis G.R., Thill G.P.
Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NRRL Y-11430.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14126 Genomic DNA. Translation: AAA67001.1.
X56180 Genomic DNA. Translation: CAA39641.1.
PIRS51513.

3D structure databases

ProteinModelPortalP45353.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP45353.

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_PICPA
AccessionPrimary (citable) accession number: P45353
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 19, 2014
This is version 91 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