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Q930I4 (HISX2_RHIME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histidinol dehydrogenase 2

Short name=HDH 2
EC=1.1.1.23
Gene names
Name:hisD2
Ordered Locus Names:RA0212
ORF Names:SMa0398
Encoded onPlasmid pSymA (megaplasmid 1)
OrganismRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]
Taxonomic identifier266834 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

Protein attributes

Sequence length456 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine By similarity. HAMAP-Rule MF_01024

Catalytic activity

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. HAMAP-Rule MF_01024

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_01024

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. HAMAP-Rule MF_01024

Sequence similarities

Belongs to the histidinol dehydrogenase family.

Caution

The conserved zinc-binding site Asp residue in position 381 is replaced by an Asn.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termComplete proteome
Plasmid
Gene Ontology (GO)
   Biological_processhistidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: InterPro

histidinol dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 456456Histidinol dehydrogenase 2 HAMAP-Rule MF_01024
PRO_0000135833

Sites

Active site3471Proton acceptor By similarity
Active site3481Proton acceptor By similarity
Metal binding2761Zinc By similarity
Metal binding2791Zinc By similarity
Metal binding4401Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q930I4 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 958D34D91C28DEEA

FASTA45648,702
        10         20         30         40         50         60 
MTLRPQLARY KDKTMTSVSF YEYSKLNAEE KAALLRRSET DISGFIEKVA PILEAVRTEG 

        70         80         90        100        110        120 
DKALARFGRE LDKADVTEAN LKVTAAEFDA AFKLVDASVL ESVQFGIDNI RKFHEEQKPE 

       130        140        150        160        170        180 
AMWLKEIRPG AFAGDRFTPI QSVALYVPRG KGSFPSVTMM TSVPAVVAGV PNLAIVTPPA 

       190        200        210        220        230        240 
PDGSVDAATL VAARLAGVET VYKAGGAQAV AAVAYGTETV KPALKIVGPG SPWVVAAKRS 

       250        260        270        280        290        300 
LSGVIDTGLP AGPSEVMILA DDTVHGGLAA LDLLIEAEHG PDSSAYLVTH SGRVAEEALA 

       310        320        330        340        350        360 
ALPEHWARMT EQRTAFSKTV LSGKTGGIVL TSSIEESYEF VNAYAPEHLE LLSEQPFIHL 

       370        380        390        400        410        420 
GHITEASEIL MGTHTPVSIA NFSLGPNAVL PTSRWARTFG PLSVTDFVKR SSIGYVTAPA 

       430        440        450 
YPEFARHSHN LAIYEGFSSH ALAVSPVRDA YLKKGA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006469 Genomic DNA. Translation: AAK64870.1.
PIRD95288.
RefSeqNP_435458.3. NC_003037.1.

3D structure databases

ProteinModelPortalQ930I4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266834.SMa0398.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK64870; AAK64870; SMa0398.
GeneID1235437.
KEGGsme:SMa0398.
PATRIC23626884. VBISinMel96828_0220.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAWVVAAKR.
OrthoDBEOG6CVVCR.
ProtClustDBPRK12447.

Enzyme and pathway databases

BioCycSMEL266834:GJF6-5220-MONOMER.
UniPathwayUPA00031; UER00014.

Family and domain databases

HAMAPMF_01024. HisD.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000099. Histidinol_dh. 1 hit.
PRINTSPR00083. HOLDHDRGNASE.
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR00069. hisD. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHISX2_RHIME
AccessionPrimary (citable) accession number: Q930I4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: December 1, 2001
Last modified: February 19, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways