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Q3M5D3 (HISX2_ANAVT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. 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 2

Short name=HDH 2
EC=1.1.1.23
Gene names
Name:hisD2
Ordered Locus Names:Ava_4204
OrganismAnabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]
Taxonomic identifier240292 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena

Protein attributes

Sequence length433 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 – 433433Histidinol dehydrogenase 2 HAMAP-Rule MF_01024
PRO_0000229849

Sites

Active site3281Proton acceptor By similarity
Active site3291Proton acceptor By similarity
Metal binding2601Zinc By similarity
Metal binding2631Zinc By similarity
Metal binding3621Zinc By similarity
Metal binding4211Zinc By similarity
Binding site1301NAD By similarity
Binding site1921NAD By similarity
Binding site2151NAD By similarity
Binding site2381Substrate By similarity
Binding site2601Substrate By similarity
Binding site2631Substrate By similarity
Binding site3291Substrate By similarity
Binding site3621Substrate By similarity
Binding site4161Substrate By similarity
Binding site4211Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3M5D3 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: 5C294698068A3ABA

FASTA43346,701
        10         20         30         40         50         60 
MLRIITQQAD VKAELQRICD RTHDEQVLHK EATVREVLQA VKRQGDKAVL HYTDEFDNQI 

        70         80         90        100        110        120 
LKAEELRVTG SELDAAYQQV SKELLEAIQL ASRQIEAFHR QRVPKSWVHF GDDDIVLGKR 

       130        140        150        160        170        180 
YTPVDRAGLY VPGGRAAYVS TVLMNAIPAK VAGVPRIVMA TPPGAQKAIN PAVLVAAQEV 

       190        200        210        220        230        240 
GVQEIYRVGG AQAIAALAYG TETIPKVDVI TGPGNIYVTL AKKLVYGTVG IDSLAGPSEV 

       250        260        270        280        290        300 
LIIADEGANP VHVATDMLAQ AEHDPMAAAI LFTTDPALAK NVQVAVERQL VDHPRRIDTE 

       310        320        330        340        350        360 
KAIAHYGLIV LVESLDAAAE LSNEFAPEHL ELEVKDPWAV LPNIRHAGAI FLGYSTPEAV 

       370        380        390        400        410        420 
GDYLAGPNHT LPTSGAARYA SALSVETFLK HSSIIQYSQT ALNKVAGAID ALATAEGLPS 

       430 
HADSVKRRIQ QDE 

« Hide

References

[1]"Complete sequence of Anabaena variabilis ATCC 29413."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29413 / PCC 7937.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000117 Genomic DNA. Translation: ABA23803.1.
RefSeqYP_324698.1. NC_007413.1.

3D structure databases

ProteinModelPortalQ3M5D3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING240292.Ava_4204.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA23803; ABA23803; Ava_4204.
GeneID3680948.
KEGGava:Ava_4204.
PATRIC35429761. VBIAnaVar43351_5410.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAFHRQRLP.
OrthoDBEOG6CVVCR.
ProtClustDBPRK00877.

Enzyme and pathway databases

BioCycAVAR240292:GCY3-4253-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 nameHISX2_ANAVT
AccessionPrimary (citable) accession number: Q3M5D3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: October 25, 2005
Last modified: February 19, 2014
This is version 65 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