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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.
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.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi667 – 6671ZincBy similarity
Metal bindingi670 – 6701ZincBy similarity
Active sitei736 – 7361By similarity
Active sitei737 – 7371By similarity
Metal bindingi769 – 7691ZincBy similarity
Metal bindingi828 – 8281ZincBy 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
OrganismiKomagataella pastoris (Yeast) (Pichia pastoris)
Taxonomic identifieri4922 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPhaffomycetaceaeKomagataella

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 842842Histidine biosynthesis trifunctional proteinPRO_0000135912Add
BLAST

Proteomic databases

PRIDEiP45353.

Structurei

3D structure databases

ProteinModelPortaliP45353.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 275275Phosphoribosyl-AMP cyclohydrolaseAdd
BLAST
Regioni276 – 35782Phosphoribosyl-ATP pyrophosphohydrolaseAdd
BLAST
Regioni358 – 842485Histidinol dehydrogenaseAdd
BLAST

Sequence similaritiesi

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

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

        10         20         30         40         50
MTFPLLPAYA SVAEFDNSLS LVGKAVFPYA ADQLHNLIKF TQSTELQVNV
60 70 80 90 100
QVESSVTEDQ FEELIDNLLK LYNNGINEVI LDLDLAERVV QRIPGARVIY
110 120 130 140 150
RTLVDKVASL PANASIAVPF SSPLGDLKSF TNGGSRTVYA FSETAKLVDV
160 170 180 190 200
TSTVASGIIP IIDARQLTTE YELSEDVKKF PVSEILLASL TTDRPDGLFT
210 220 230 240 250
TLVADSSNYS LGLVYSSKKS IPEAIRTQTG VYQSRRHGLW YKGATSGATQ
260 270 280 290 300
KLLGIELDCD GDCLKFVVEQ TGVGFCHLER TSCFGQSKGL RAMEATLWDR
310 320 330 340 350
KSNAPEGSYT KRLFDDEVLL NAKIREEADE LAEAKSKEDI AWECADLFYF
360 370 380 390 400
ALVRCAKYGV TLDEVERNLD MKSLKVTRRK GDAKPGYTKE QPKEESKPKE
410 420 430 440 450
VPSEGRIELC KIDVSKASSQ EIEDALRRPI QKTEQIMELV KPIVDNVRQN
460 470 480 490 500
GDKALLELTA KFDGVALKTP VLEAPFPEEL MQLPDNVKRA IDLSIDNVRK
510 520 530 540 550
FHEAQLAETL QVETCPGVVC SRFARPIEKV GLYIPGGTAI LPSTSLMLGV
560 570 580 590 600
PAKVAGCKEI VFASPPKKDG TLTPEVIYVA HKVGAKCIVL AGGAQAVAAM
610 620 630 640 650
AYGTETVPKC DKIFGPGNQF VTAAKMMVQN DTSALCSIDM PAGPSEVLVI
660 670 680 690 700
ADKYADPDFV VSDLLSQAEH GIDSQVILLA VDMTDKELAR IEDAVHNQAV
710 720 730 740 750
QLPRVEIVRK CIAHSTTLSV ATYEQALEMS NQYAPEHLIL QIENASYVDQ
760 770 780 790 800
VQHAGSVFVG AYSPESCGDY SSGTNHTLPT YGYARQYSGV NTATFQKFIT
810 820 830 840
SQDVTPEGLK HIGQAVMDLA AVEGLDAHRN AVKVRMEKLG LI
Length:842
Mass (Da):91,942
Last modified:November 1, 1995 - v1
Checksum:i67DA24E2266A4A3E
GO

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14126 Genomic DNA. Translation: AAA67001.1.
X56180 Genomic DNA. Translation: CAA39641.1.
PIRiS51513.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 94 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