Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q2RQM7 (HISX_RHORT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 62. 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

Short name=HDH
EC=1.1.1.23
Gene names
Name:hisD
Ordered Locus Names:Rru_A2771
OrganismRhodospirillum rubrum (strain ATCC 11170 / NCIB 8255) [Reference proteome] [HAMAP]
Taxonomic identifier269796 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum

Protein attributes

Sequence length434 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.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
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: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 434434Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000229865

Sites

Active site3281Proton acceptor By similarity
Active site3291Proton acceptor By similarity
Metal binding2591Zinc By similarity
Metal binding2621Zinc By similarity
Metal binding3621Zinc By similarity
Metal binding4211Zinc By similarity
Binding site1301NAD By similarity
Binding site1911NAD By similarity
Binding site2141NAD By similarity
Binding site2371Substrate By similarity
Binding site2591Substrate By similarity
Binding site2621Substrate By similarity
Binding site3291Substrate By similarity
Binding site3621Substrate By similarity
Binding site4161Substrate By similarity
Binding site4211Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2RQM7 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: BB30BB3A879BB054

FASTA43445,648
        10         20         30         40         50         60 
MPLRLEASSA DFAPAFAALL AGKRESAQDV NDVVSAILAD VRLRGDDALI DYTARFDKMT 

        70         80         90        100        110        120 
VSAEGLRFSD DEVDTAVALI EPALRDALAL AAKRITRFHE RQMPTAISFT DEDGVRLGQR 

       130        140        150        160        170        180 
WTAVSAAGLY VPGGLAAYPS SVLMNALPAK VAGVERLVMV VPTPAGRINP LVLAAAKLAG 

       190        200        210        220        230        240 
VDEIYRVGGA QAVAALAYGT RTIAPVDKIV GPGNAYVAAA KRQVFGTVGI DMIAGPSEIL 

       250        260        270        280        290        300 
VVADGANDPD WIALDLLSQA EHDAAAQSIL ITDDRAFADR VERAVTDRLR TLSRTEIASA 

       310        320        330        340        350        360 
SWRDHGAIIL VGDLLRDAPA LVDKVAPEHL ELAVADPDAL AARVRHAGAI FLGRYTPEAI 

       370        380        390        400        410        420 
GDYIAGPNHV LPTSRTARFS SGLGVLDFMK RTTLVGCGAE SLGAIGPSAV RLARAEGLEA 

       430 
HGLSVAARMN RGWE 

« Hide

References

[1]"Complete sequence of the chromosome of Rhodospirillum rubrum ATCC 11170."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., Reslewic S., Zhou S., Schwartz D.C.
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000230 Genomic DNA. Translation: ABC23568.1.
RefSeqYP_427855.1. NC_007643.1.

3D structure databases

ProteinModelPortalQ2RQM7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269796.Rru_A2771.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC23568; ABC23568; Rru_A2771.
GeneID3836211.
KEGGrru:Rru_A2771.
PATRIC23329288. VBIRhoRub82919_2877.

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAPSEILII.
OrthoDBEOG6CVVCR.
ProtClustDBPRK00877.

Enzyme and pathway databases

BioCycRRUB269796:GCN1-2819-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 nameHISX_RHORT
AccessionPrimary (citable) accession number: Q2RQM7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: January 24, 2006
Last modified: February 19, 2014
This is version 62 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