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Q8GDP4

- HISX_HELMO

UniProt

Q8GDP4 - HISX_HELMO

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Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Heliobacillus mobilis
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.UniRule annotation

Catalytic activityi

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei126 – 1261NADUniRule annotation
Binding sitei188 – 1881NADUniRule annotation
Binding sitei210 – 2101NADUniRule annotation
Binding sitei233 – 2331SubstrateUniRule annotation
Metal bindingi255 – 2551ZincUniRule annotation
Binding sitei255 – 2551SubstrateUniRule annotation
Metal bindingi258 – 2581ZincUniRule annotation
Binding sitei258 – 2581SubstrateUniRule annotation
Active sitei323 – 3231Proton acceptorUniRule annotation
Active sitei324 – 3241Proton acceptorUniRule annotation
Binding sitei324 – 3241SubstrateUniRule annotation
Metal bindingi357 – 3571ZincUniRule annotation
Binding sitei357 – 3571SubstrateUniRule annotation
Binding sitei411 – 4111SubstrateUniRule annotation
Metal bindingi416 – 4161ZincUniRule annotation
Binding sitei416 – 4161SubstrateUniRule annotation

GO - Molecular functioni

  1. histidinol dehydrogenase activity Source: UniProtKB-EC
  2. NAD binding Source: InterPro
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. histidine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

UniPathwayiUPA00031; UER00014.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol dehydrogenaseUniRule annotation (EC:1.1.1.23UniRule annotation)
Short name:
HDHUniRule annotation
Gene namesi
Name:hisDUniRule annotation
OrganismiHeliobacillus mobilis
Taxonomic identifieri28064 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesHeliobacteriaceaeHeliobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›426›426Histidinol dehydrogenasePRO_0000135780Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ8GDP4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Family and domain databases

HAMAPiMF_01024. HisD.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamiPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000099. Histidinol_dh. 1 hit.
PRINTSiPR00083. HOLDHDRGNASE.
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR00069. hisD. 1 hit.
PROSITEiPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q8GDP4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVRLITYPSI DADNYLQKKT LDDANVSVQV AQVLETIRCR GVEAVFEYTK
60 70 80 90 100
RFDGATVNEA NFRVSEAEID EAYSKVDPEV LAALRRARDN IRRYHEKQLR
110 120 130 140 150
PSWIEPEADG TMLGQLIRPL ERVGTYVPGG LASYPSSVLM NAVPAKVAGV
160 170 180 190 200
PQVVMATPPG KDGSINPYTL VAAREAGVDE IYRMGGAQAV AAMAYGAGLK
210 220 230 240 250
AVDKITGPGN IYVTLAKKQV YGTVDIDMLA GPSEILVIAD ETAPPAYVAA
260 270 280 290 300
DFLSQVEHDV RAAAVLVTPS EILARAVEGE IQRQMDYLPR REIMEQALKD
310 320 330 340 350
NSAVIVVKDL DEACEVANRY APEHLEVLTK EPFALLGKLT QAGAIFLGPY
360 370 380 390 400
SPEPVGDYYA GPNHVLPTGG TARFYSPLNV DTFMKKTSVI AYSKARFEQA
410 420
ADDILALAKC EGLDAHANAV AVRIEK
Length:426
Mass (Da):46,201
Last modified:March 1, 2003 - v1
Checksum:i8DF8698277EB8A1E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei426 – 4261

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY142932 Genomic DNA. Translation: AAN87536.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY142932 Genomic DNA. Translation: AAN87536.1 .

3D structure databases

ProteinModelPortali Q8GDP4.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00014 .

Family and domain databases

HAMAPi MF_01024. HisD.
InterProi IPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view ]
Pfami PF00815. Histidinol_dh. 1 hit.
[Graphical view ]
PIRSFi PIRSF000099. Histidinol_dh. 1 hit.
PRINTSi PR00083. HOLDHDRGNASE.
SUPFAMi SSF53720. SSF53720. 1 hit.
TIGRFAMsi TIGR00069. hisD. 1 hit.
PROSITEi PS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiHISX_HELMO
AccessioniPrimary (citable) accession number: Q8GDP4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 1, 2003
Last modified: November 26, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3