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

Q9CLM4 (HISX_PASMU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 82. 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:PM1198
OrganismPasteurella multocida (strain Pm70) [Complete proteome] [HAMAP]
Taxonomic identifier272843 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella

Protein attributes

Sequence length428 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
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 – 428428Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135808

Sites

Active site3211Proton acceptor By similarity
Active site3221Proton acceptor By similarity
Metal binding2541Zinc By similarity
Metal binding2571Zinc By similarity
Metal binding3551Zinc By similarity
Metal binding4141Zinc By similarity
Binding site1271NAD By similarity
Binding site1851NAD By similarity
Binding site2081NAD By similarity
Binding site2321Substrate By similarity
Binding site2541Substrate By similarity
Binding site2571Substrate By similarity
Binding site3221Substrate By similarity
Binding site3551Substrate By similarity
Binding site4091Substrate By similarity
Binding site4141Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CLM4 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 583D332D94F1F4AF

FASTA42846,150
        10         20         30         40         50         60 
MQTLIWNTLN SAQKQAALSR PAQAVGEQIT QAVNAIKSNV INNGDKALFE LAEKFDKTTL 

        70         80         90        100        110        120 
ESLVISKAQV EQASQRIATE LKQAIQTAKG NIERFHQAQK NQTVDLETQA GVRCQVVTRP 

       130        140        150        160        170        180 
IQNVGLYIPG GSAPLFSTVL MLAVPAKIAG CKTIVLCSPP PIADEILYTA NLCGVETIYA 

       190        200        210        220        230        240 
IGGAQAIFAM ANGTESVQKV DKIFGPGNAF VTEAKRQVLQ QGTAIDMPAG PSEVLVIADE 

       250        260        270        280        290        300 
FADPDFVASD LLSQAEHGSD SQVILVTNCE TLAKQTALSI EQQLARLPRA ETARKALAHS 

       310        320        330        340        350        360 
RTFIAEDLQQ CVEISNAYAP EHLVVQVENA RNLLPFLDNA GSIFLGAYSP ESMGDYASGT 

       370        380        390        400        410        420 
NHVLPTYGYT RTHSSLGLAD FSKRMTVQEL TPQGFKDLAN TVMLMAEAEQ LEAHKQAVAI 


RLEKLTQE 

« Hide

References

[1]"Complete genomic sequence of Pasteurella multocida Pm70."
May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pm70.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004439 Genomic DNA. Translation: AAK03282.1.
RefSeqNP_246135.1. NC_002663.1.

3D structure databases

ProteinModelPortalQ9CLM4.
SMRQ9CLM4. Positions 6-428.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272843.PM1198.

Proteomic databases

PRIDEQ9CLM4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK03282; AAK03282; PM1198.
GeneID1244545.
KEGGpmu:PM1198.
PATRIC22871649. VBIPasMul88067_1209.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMADEMAMPI.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

BioCycPMUL272843:GC8W-1248-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_PASMU
AccessionPrimary (citable) accession number: Q9CLM4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: June 1, 2001
Last modified: May 14, 2014
This is version 82 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