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Protein

Histidine biosynthesis trifunctional protein

Gene

HIS4

Organism
Komagataella pastoris (Yeast) (Pichia pastoris)
Status
Reviewed-Annotation score: 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: L-histidine biosynthesis

This protein is involved in step 2, 3 and 9 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Histidine biosynthesis trifunctional protein (HIS4)
  3. Histidine biosynthesis trifunctional protein (HIS4)
  4. no protein annotated in this organism
  5. no protein annotated in this organism
  6. Imidazoleglycerol-phosphate dehydratase (HIS3), Imidazoleglycerol-phosphate dehydratase (HIS3)
  7. no protein annotated in this organism
  8. no protein annotated in this organism
  9. Histidine biosynthesis trifunctional protein (HIS4)
This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi667ZincBy similarity1
Metal bindingi670ZincBy similarity1
Active sitei736By similarity1
Active sitei737By similarity1
Metal bindingi769ZincBy similarity1
Metal bindingi828ZincBy similarity1

GO - Molecular functioni

GO - Biological processi

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001359121 – 842Histidine biosynthesis trifunctional proteinAdd BLAST842

Proteomic databases

PRIDEiP45353.

Interactioni

Protein-protein interaction databases

STRINGi644223.XP_002490271.1.

Structurei

3D structure databases

ProteinModelPortaliP45353.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 275Phosphoribosyl-AMP cyclohydrolaseAdd BLAST275
Regioni276 – 357Phosphoribosyl-ATP pyrophosphohydrolaseAdd BLAST82
Regioni358 – 842Histidinol dehydrogenaseAdd BLAST485

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2697. Eukaryota.
KOG4311. Eukaryota.
COG0139. LUCA.
COG0140. LUCA.
COG0141. LUCA.

Family and domain databases

CDDicd06572. Histidinol_dh. 1 hit.
HAMAPiMF_01024. HisD. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR008179. HisE.
IPR016298. Histidine_synth_trifunct.
IPR001692. Histidinol_DH_CS.
IPR012131. Hstdl_DH.
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)DescriptionActionsGraphical viewLength
Sequence conflicti92R → RM (Ref. 2) Curated1
Sequence conflicti507A → T in CAA39641 (Ref. 2) Curated1
Sequence conflicti661V → A in CAA39641 (Ref. 2) Curated1
Sequence conflicti746S → SS in CAA39641 (Ref. 2) Curated1

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.
PIRiS51513.

3D structure databases

ProteinModelPortaliP45353.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi644223.XP_002490271.1.

Proteomic databases

PRIDEiP45353.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG2697. Eukaryota.
KOG4311. Eukaryota.
COG0139. LUCA.
COG0140. LUCA.
COG0141. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00007.
UPA00031; UER00008.
UPA00031; UER00014.

Family and domain databases

CDDicd06572. Histidinol_dh. 1 hit.
HAMAPiMF_01024. HisD. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR008179. HisE.
IPR016298. Histidine_synth_trifunct.
IPR001692. Histidinol_DH_CS.
IPR012131. Hstdl_DH.
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]
ProtoNetiSearch...

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: September 7, 2016
This is version 98 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.