Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q5KVC6

- HISX_GEOKA

UniProt

Q5KVC6 - HISX_GEOKA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Histidinol dehydrogenase

Gene

hisD

Organism
Geobacillus kaustophilus (strain HTA426)
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 sitei121 – 1211NADUniRule annotation
Binding sitei183 – 1831NADUniRule annotation
Binding sitei206 – 2061NADUniRule annotation
Binding sitei229 – 2291SubstrateUniRule annotation
Metal bindingi251 – 2511ZincUniRule annotation
Binding sitei251 – 2511SubstrateUniRule annotation
Metal bindingi254 – 2541ZincUniRule annotation
Binding sitei254 – 2541SubstrateUniRule annotation
Active sitei319 – 3191Proton acceptorUniRule annotation
Active sitei320 – 3201Proton acceptorUniRule annotation
Binding sitei320 – 3201SubstrateUniRule annotation
Metal bindingi353 – 3531ZincUniRule annotation
Binding sitei353 – 3531SubstrateUniRule annotation
Binding sitei407 – 4071SubstrateUniRule annotation
Metal bindingi412 – 4121ZincUniRule annotation
Binding sitei412 – 4121SubstrateUniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. histidine biosynthetic process Source: UniProtKB-HAMAP
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

BioCyciGKAU235909:GJO7-3188-MONOMER.
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
Ordered Locus Names:GK3075
OrganismiGeobacillus kaustophilus (strain HTA426)
Taxonomic identifieri235909 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus
ProteomesiUP000001172: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 424424Histidinol dehydrogenasePRO_0000135773Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi235909.GK3075.

Structurei

3D structure databases

ProteinModelPortaliQ5KVC6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidinol dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0141.
HOGENOMiHOG000243914.
KOiK00013.
OMAiYAAKLCG.
OrthoDBiEOG6CVVCR.

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: Complete.

Q5KVC6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKIERIRGGV SLRRTIESGT EEQRRAVLDI IANVRDRGDA ALKEYTERFD
60 70 80 90 100
GVKLDSLKVT EEEMKRAHAA MDAEMLEIIR QAAANIRDYH KRQKRESWWM
110 120 130 140 150
TKEDGTILGQ KVTPLDAVGL YVPGGTAAYP SSVLMNVIPA QVAGVKRIVI
160 170 180 190 200
TSPPNKDGTL PAGVLAAAYE LGVTEIYKVG GAQAIAALAY GTETIRPVDK
210 220 230 240 250
IFGPGNIYVA LAKREVFGHV AIDMIAGPSE IVVLADETAR PDEIAADLLS
260 270 280 290 300
QAEHDVRASA ILVTPSMKLA LAVASEVERQ LETLPRRDIA QAALENYGAI
310 320 330 340 350
YVTETLEEAV DVVNELAPEH LEVMTAEPLA LFGRLRHAGA MFFGRFSSEP
360 370 380 390 400
VGDYFAGPNH VLPTNGTARF SSGLSVDEFV KKSSVIVYSE TALKQHGDKI
410 420
AAFARLEGLE AHARAIEVRL EKGE
Length:424
Mass (Da):46,055
Last modified:February 1, 2005 - v1
Checksum:iDDD2807E49EB959D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000043 Genomic DNA. Translation: BAD77360.1.
RefSeqiYP_148928.1. NC_006510.1.

Genome annotation databases

EnsemblBacteriaiBAD77360; BAD77360; GK3075.
GeneIDi3184204.
KEGGigka:GK3075.
PATRICi21967704. VBIGeoKau81518_3282.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000043 Genomic DNA. Translation: BAD77360.1 .
RefSeqi YP_148928.1. NC_006510.1.

3D structure databases

ProteinModelPortali Q5KVC6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 235909.GK3075.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD77360 ; BAD77360 ; GK3075 .
GeneIDi 3184204.
KEGGi gka:GK3075.
PATRICi 21967704. VBIGeoKau81518_3282.

Phylogenomic databases

eggNOGi COG0141.
HOGENOMi HOG000243914.
KOi K00013.
OMAi YAAKLCG.
OrthoDBi EOG6CVVCR.

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00014 .
BioCyci GKAU235909:GJO7-3188-MONOMER.

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. "Thermoadaptation trait revealed by the genome sequence of thermophilic Geobacillus kaustophilus."
    Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H., Matsui S., Uchiyama I.
    Nucleic Acids Res. 32:6292-6303(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HTA426.

Entry informationi

Entry nameiHISX_GEOKA
AccessioniPrimary (citable) accession number: Q5KVC6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: February 1, 2005
Last modified: November 26, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3