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Q987C6 (HISX3_RHILO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 78. 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 3

Short name=HDH 3
EC=1.1.1.23
Gene names
Name:hisD3
Ordered Locus Names:mlr7107
OrganismRhizobium loti (strain MAFF303099) (Mesorhizobium loti) [Complete proteome] [HAMAP]
Taxonomic identifier266835 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium

Protein attributes

Sequence length440 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 367 is replaced by an Asn.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termComplete 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: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 440440Histidinol dehydrogenase 3 HAMAP-Rule MF_01024
PRO_0000135831

Sites

Active site3331Proton acceptor By similarity
Active site3341Proton acceptor By similarity
Metal binding2621Zinc By similarity
Metal binding2651Zinc By similarity
Metal binding4261Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q987C6 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 76FF8FD9E42CA90C

FASTA44047,089
        10         20         30         40         50         60 
MSDVSFHDLS SLDATQRSSL LKRAEADLSV FVEKVRPIIQ AVKDEGDAAL IRFARELDKA 

        70         80         90        100        110        120 
NVAEGGLQVS EAEFDAAFDK VEKDVVESIG FGIDNIRRFH EEQKPETMWL KEVRPGAYAG 

       130        140        150        160        170        180 
DRYTPIASVA LYVPRGKGAF PSVTMMTSVP AVIAGVPQIA IVTPPTSDGS VDAATLVAAR 

       190        200        210        220        230        240 
LAGVHTVYKC GGAQAVAAVA YGTETVKPAL KIVGPGSPWV VAAKSELSSI INTGLPAGPS 

       250        260        270        280        290        300 
EAIIFADDSV DGGLAALDLL IEAEHGPDSS AYLVTHSRKV AEAALAALPQ HWSRMTEQRV 

       310        320        330        340        350        360 
EFSRAVLTGK RGGIVLTASL EDSYRFINDY APEHLEILSK EPFAHLGHIT EAAEILMGPH 

       370        380        390        400        410        420 
TPVTLANFVL GPNAVLPTSR WARTYGPLSV TDFVKRSSVG YVTSAAYPEL AKHARRLARY 

       430        440 
EGFSSHENAV SEIRDRYLAG 

« Hide

References

[1]"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti."
Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. expand/collapse author list , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.
DNA Res. 7:331-338(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF303099.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000012 Genomic DNA. Translation: BAB53277.1.
RefSeqNP_107491.1. NC_002678.2.

3D structure databases

ProteinModelPortalQ987C6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266835.mlr7107.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB53277; BAB53277; BAB53277.
GeneID1230146.
KEGGmlo:mlr7107.
PATRIC22485579. VBIMesLot2464_5669.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycMLOT266835:GJ9L-5642-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 nameHISX3_RHILO
AccessionPrimary (citable) accession number: Q987C6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: October 1, 2001
Last modified: February 19, 2014
This is version 78 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