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Q46J19 (HISX_PROMT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 66. 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:PMN2A_1019
OrganismProchlorococcus marinus (strain NATL2A) [Complete proteome] [HAMAP]
Taxonomic identifier59920 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length449 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 – 449449Histidinol dehydrogenase HAMAP-Rule MF_01024
PRO_0000135815

Sites

Active site3441Proton acceptor By similarity
Active site3451Proton acceptor By similarity
Metal binding2761Zinc By similarity
Metal binding2791Zinc By similarity
Metal binding3781Zinc By similarity
Metal binding4371Zinc By similarity
Binding site1461NAD By similarity
Binding site2081NAD By similarity
Binding site2311NAD By similarity
Binding site2541Substrate By similarity
Binding site2761Substrate By similarity
Binding site2791Substrate By similarity
Binding site3451Substrate By similarity
Binding site3781Substrate By similarity
Binding site4321Substrate By similarity
Binding site4371Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q46J19 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: E8D895AE8A088870

FASTA44948,862
        10         20         30         40         50         60 
MTQIINKDEV QETSSKKLTI KTANSIDQAQ FELRKITERT SGTVQDEAIK VVDDILKNVR 

        70         80         90        100        110        120 
ERGDEALTEY TSRFDGFLTE KFQVSSDLIL KAWEETPREL QDSLLLAKKR IEKFHSLQVP 

       130        140        150        160        170        180 
KNITYTGPNG ETLGRRWSPV EKAGIYVPGG RAAYPSTVLM NAIPAYVAGV NQIIMVSPAN 

       190        200        210        220        230        240 
SQGEINQTVL AAAHITGINK IFRLGGAQAI CALASGTESI PKVDVITGPG NIYVTLAKKK 

       250        260        270        280        290        300 
VYGKVGIDSL AGPSEILIIA DQSAKLEHVA SDMLAQSEHD PLASAILITT NTKLAEKLPA 

       310        320        330        340        350        360 
EINRQLINHP RLKICQESIS NWGLIVLCDD LETCAQLSDT FAPEHLELLV EDPKKLSESI 

       370        380        390        400        410        420 
NNAGAIFMGP WSPEAIGDYL GGPNHTLPTS GTARFAGALG VETFMKNTSL IDFSKEAFNE 

       430        440 
NKNAVVQLAN SEGLHSHAES IRIRDSKSF 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NATL2A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000095 Genomic DNA. Translation: AAZ58509.1.
RefSeqYP_292212.1. NC_007335.2.

3D structure databases

ProteinModelPortalQ46J19.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59920.PMN2A_1019.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ58509; AAZ58509; PMN2A_1019.
GeneID3606405.
KEGGpmn:PMN2A_1019.
PATRIC23025877. VBIProMar14922_1866.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAYAAKLCG.
OrthoDBEOG6CVVCR.
PhylomeDBQ46J19.

Enzyme and pathway databases

BioCycPMAR59920:GI1O-1890-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_PROMT
AccessionPrimary (citable) accession number: Q46J19
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: September 13, 2005
Last modified: July 9, 2014
This is version 66 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