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P45353

- HIS2_PICPA

UniProt

P45353 - HIS2_PICPA

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Protein
Histidine biosynthesis trifunctional protein
Gene
HIS4
Organism
Komagataella pastoris (Yeast) (Pichia pastoris)
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 bindingi667 – 6671Zinc By similarity
Metal bindingi670 – 6701Zinc By similarity
Active sitei736 – 7361 By similarity
Active sitei737 – 7371 By similarity
Metal bindingi769 – 7691Zinc By similarity
Metal bindingi828 – 8281Zinc By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. NAD binding Source: InterPro
  3. histidinol dehydrogenase activity Source: UniProtKB-EC
  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
OrganismiKomagataella pastoris (Yeast) (Pichia pastoris)
Taxonomic identifieri4922 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKomagataella

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 842842Histidine biosynthesis trifunctional proteinUniRule annotation
PRO_0000135912Add
BLAST

Proteomic databases

PRIDEiP45353.

Structurei

3D structure databases

ProteinModelPortaliP45353.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 275275Phosphoribosyl-AMP cyclohydrolaseUniRule annotation
Add
BLAST
Regioni276 – 35782Phosphoribosyl-ATP pyrophosphohydrolaseUniRule annotation
Add
BLAST
Regioni358 – 842485Histidinol dehydrogenaseUniRule annotation
Add
BLAST

Sequence similaritiesi

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

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.

P45353-1 [UniParc]FASTAAdd to Basket

« Hide

MTFPLLPAYA SVAEFDNSLS LVGKAVFPYA ADQLHNLIKF TQSTELQVNV    50
QVESSVTEDQ FEELIDNLLK LYNNGINEVI LDLDLAERVV QRIPGARVIY 100
RTLVDKVASL PANASIAVPF SSPLGDLKSF TNGGSRTVYA FSETAKLVDV 150
TSTVASGIIP IIDARQLTTE YELSEDVKKF PVSEILLASL TTDRPDGLFT 200
TLVADSSNYS LGLVYSSKKS IPEAIRTQTG VYQSRRHGLW YKGATSGATQ 250
KLLGIELDCD GDCLKFVVEQ TGVGFCHLER TSCFGQSKGL RAMEATLWDR 300
KSNAPEGSYT KRLFDDEVLL NAKIREEADE LAEAKSKEDI AWECADLFYF 350
ALVRCAKYGV TLDEVERNLD MKSLKVTRRK GDAKPGYTKE QPKEESKPKE 400
VPSEGRIELC KIDVSKASSQ EIEDALRRPI QKTEQIMELV KPIVDNVRQN 450
GDKALLELTA KFDGVALKTP VLEAPFPEEL MQLPDNVKRA IDLSIDNVRK 500
FHEAQLAETL QVETCPGVVC SRFARPIEKV GLYIPGGTAI LPSTSLMLGV 550
PAKVAGCKEI VFASPPKKDG TLTPEVIYVA HKVGAKCIVL AGGAQAVAAM 600
AYGTETVPKC DKIFGPGNQF VTAAKMMVQN DTSALCSIDM PAGPSEVLVI 650
ADKYADPDFV VSDLLSQAEH GIDSQVILLA VDMTDKELAR IEDAVHNQAV 700
QLPRVEIVRK CIAHSTTLSV ATYEQALEMS NQYAPEHLIL QIENASYVDQ 750
VQHAGSVFVG AYSPESCGDY SSGTNHTLPT YGYARQYSGV NTATFQKFIT 800
SQDVTPEGLK HIGQAVMDLA AVEGLDAHRN AVKVRMEKLG LI 842
Length:842
Mass (Da):91,942
Last modified:November 1, 1995 - v1
Checksum:i67DA24E2266A4A3E
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921R → RM1 Publication
Sequence conflicti507 – 5071A → T in CAA39641. 1 Publication
Sequence conflicti661 – 6611V → A in CAA39641. 1 Publication
Sequence conflicti746 – 7461S → SS in CAA39641. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U14126 Genomic DNA. Translation: AAA67001.1.
X56180 Genomic DNA. Translation: CAA39641.1.
PIRiS51513.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U14126 Genomic DNA. Translation: AAA67001.1 .
X56180 Genomic DNA. Translation: CAA39641.1 .
PIRi S51513.

3D structure databases

ProteinModelPortali P45353.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P45353.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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

  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.

Entry informationi

Entry nameiHIS2_PICPA
AccessioniPrimary (citable) accession number: P45353
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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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