SubmitCancel

Skip Header

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

Q9RQ82

- HISX_BUCMH

UniProt

Q9RQ82 - HISX_BUCMH

(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
Buchnera aphidicola subsp. Melaphis rhois
Status
Reviewed - Annotation score: 2 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 By similarity.

Catalytic activityi

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

Cofactori

Binds 1 zinc ion per subunit By similarity.

Pathwayi

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 dehydrogenase (EC:1.1.1.23)
Short name:
HDH
Gene namesi
Name:hisD
OrganismiBuchnera aphidicola subsp. Melaphis rhois
Taxonomic identifieri118103 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›201›201Histidinol dehydrogenasePRO_0000135745Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ9RQ82.
SMRiQ9RQ82. Positions 6-201.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiIPR016161. Ald_DH/histidinol_DH.
IPR012131. Hstdl_DH.
[Graphical view]
PfamiPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PRINTSiPR00083. HOLDHDRGNASE.
SUPFAMiSSF53720. SSF53720. 1 hit.

Sequencei

Sequence statusi: Fragment.

Q9RQ82-1 [UniParc]FASTAAdd to Basket

« Hide

MKNCLKIIHW DRCSIEEREK ILSRPILDDL SAIKKQVKTI ISDVNSLGDQ    50
ALYNYTNIFD KIKLNNIKIS HQDLVKAELC IDVKAKNAIQ VAIDNIRTFH 100
ISQNISTLNI EINKGIYCQQ IVRPIGSVGL YIPGGSAPLL STVLMLAIPA 150
RIAGCKKIVL CSPPPITNEV LYASKICGVQ EIFQVGGAQA IAALGFGTET 200
I 201
Length:201
Mass (Da):22,028
Last modified:May 1, 2000 - v1
Checksum:iE0FA5769CF7DB395
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei201 – 2011

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF129283 Genomic DNA. Translation: AAF13776.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF129283 Genomic DNA. Translation: AAF13776.1 .

3D structure databases

ProteinModelPortali Q9RQ82.
SMRi Q9RQ82. Positions 6-201.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00014 .

Family and domain databases

InterProi IPR016161. Ald_DH/histidinol_DH.
IPR012131. Hstdl_DH.
[Graphical view ]
Pfami PF00815. Histidinol_dh. 1 hit.
[Graphical view ]
PRINTSi PR00083. HOLDHDRGNASE.
SUPFAMi SSF53720. SSF53720. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Sequence evolution in bacterial endosymbionts having extreme base compositions."
    Clark M.A., Moran N.A., Baumann P.
    Mol. Biol. Evol. 16:1586-1598(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiHISX_BUCMH
AccessioniPrimary (citable) accession number: Q9RQ82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 59 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

Similar proteinsi