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Q3MEV7 (HISX1_ANAVT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 62. 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 1

Short name=HDH 1
EC=1.1.1.23
Gene names
Name:hisD1
Ordered Locus Names:Ava_0855
OrganismAnabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]
Taxonomic identifier240292 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena

Protein attributes

Sequence length431 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 – 431431Histidinol dehydrogenase 1 HAMAP-Rule MF_01024
PRO_0000229848

Sites

Active site3241Proton acceptor By similarity
Active site3251Proton acceptor By similarity
Metal binding2561Zinc By similarity
Metal binding2591Zinc By similarity
Metal binding3581Zinc By similarity
Metal binding4171Zinc By similarity
Binding site1271NAD By similarity
Binding site1881NAD By similarity
Binding site2111NAD By similarity
Binding site2341Substrate By similarity
Binding site2561Substrate By similarity
Binding site2591Substrate By similarity
Binding site3251Substrate By similarity
Binding site3581Substrate By similarity
Binding site4121Substrate By similarity
Binding site4171Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3MEV7 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: D3AC6AF531ED1B1A

FASTA43145,806
        10         20         30         40         50         60 
MLVLKTTDQE FSTRFQSLVS DRREATVDVS GTVRDILAHV KAHGDAAVQE YTSRFDHYSP 

        70         80         90        100        110        120 
HSHHLSAAFI AEQAAKCSAE VKAAIELAAE RISSFHQKQL PQDIGYTDTV GVKLGLNWVA 

       130        140        150        160        170        180 
LSQVGIYVPG GRASYPSSVL MNALPAKIAG VERIVMTVPM PHGEINPAVL AAAQVAGVTE 

       190        200        210        220        230        240 
IYSIGGAQAV GALAYGTETI TPVDKIVGPG NAYVAEAKRQ VFGTVGIDSI AGPSEILVVA 

       250        260        270        280        290        300 
DRQNNPEWIA WDLLSQAEHD PSAQSILITD SESFAQQVIG AVEQILTTLP TTKVASSSWQ 

       310        320        330        340        350        360 
NHGAVIIVRD LAESIPLLNQ LAPEHVELCV DNPQLLASQI KCAGSLFLGR YTPEAIGDYL 

       370        380        390        400        410        420 
GGPNHVLPTS RSARFASGLS VYDFLKRITY LECNQAALQA IGQSAVTLAE TEGLPAHAGS 

       430 
VAVRLQGLND M 

« 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: ABA20479.1.
RefSeqYP_321374.1. NC_007413.1.

3D structure databases

ProteinModelPortalQ3MEV7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING240292.Ava_0855.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA20479; ABA20479; Ava_0855.
GeneID3681756.
KEGGava:Ava_0855.
PATRIC35422144. VBIAnaVar43351_1637.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAERISSFH.
OrthoDBEOG6CVVCR.
ProtClustDBPRK12447.

Enzyme and pathway databases

BioCycAVAR240292:GCY3-865-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 nameHISX1_ANAVT
AccessionPrimary (citable) accession number: Q3MEV7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: October 25, 2005
Last modified: February 19, 2014
This is version 62 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