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Q65RB1 (HISX_MANSM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 73. 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:MS1892
OrganismMannheimia succiniciproducens (strain MBEL55E) [Complete proteome] [HAMAP]
Taxonomic identifier221988 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeBasfia

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_0000135793

Sites

Active site3231Proton acceptor By similarity
Active site3241Proton acceptor By similarity
Metal binding2561Zinc By similarity
Metal binding2591Zinc By similarity
Metal binding3571Zinc By similarity
Metal binding4161Zinc By similarity
Binding site1271NAD By similarity
Binding site1851NAD By similarity
Binding site2081NAD By similarity
Binding site2341Substrate By similarity
Binding site2561Substrate By similarity
Binding site2591Substrate By similarity
Binding site3241Substrate By similarity
Binding site3571Substrate By similarity
Binding site4111Substrate By similarity
Binding site4161Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65RB1 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 7923F52A6F7C11AF

FASTA42846,088
        10         20         30         40         50         60 
MQTLIWKDLT EQEKKQALTR PAISAAGNIK DAVDAIRENV VANGDKALFE LSEKFDRVKL 

        70         80         90        100        110        120 
NSLEVSEQQI EEAAQRLPEE LKQAIQNAKK NIEAFHLAQV PVEADVETQS GVRCQVLTRP 

       130        140        150        160        170        180 
INRVGLYIPG GSAPLFSTVL MLAIPAKIAG CKKIVLCSPP PIADAILYAA NLCGVETIYQ 

       190        200        210        220        230        240 
VGGAQAVVAM AFGTETVAKV DKIFGPGNAF VTEAKRQVSQ AVNGAAIDMQ AGPSEVLVLA 

       250        260        270        280        290        300 
DENADPDFVA SDLLSQAEHG ADSQVILVTP SERLALETEL AVERQLTTLP RSEIAQKALA 

       310        320        330        340        350        360 
HSRIFIAENL QQCVEISNEY APEHLVVQVQ NARDLLSNID NAGSIFLGAY SPESMGDYAS 

       370        380        390        400        410        420 
GTNHVLPTYG YTRTSSSLGL ADFSKRMTVQ ELSPQGFKDL AKTVEVMAAA ERLDAHKQAV 


SIRLAKIK 

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References

[1]"The genome sequence of the capnophilic rumen bacterium Mannheimia succiniciproducens."
Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H., Jeong H., Hur C.G., Kim J.J.
Nat. Biotechnol. 22:1275-1281(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MBEL55E.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016827 Genomic DNA. Translation: AAU38499.1.
RefSeqYP_089084.1. NC_006300.1.

3D structure databases

ProteinModelPortalQ65RB1.
SMRQ65RB1. Positions 6-428.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING221988.MS1892.

Proteomic databases

PRIDEQ65RB1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU38499; AAU38499; MS1892.
GeneID3075501.
KEGGmsu:MS1892.
PATRIC22447045. VBIManSuc86752_1729.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAGFLFHAN.
OrthoDBEOG6CVVCR.

Enzyme and pathway databases

BioCycBMAN221988:GHGM-1947-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_MANSM
AccessionPrimary (citable) accession number: Q65RB1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: October 25, 2004
Last modified: May 14, 2014
This is version 73 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