ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q47AL5

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name HISX_DECAR
Primary accession number Q47AL5
Secondary accession numbers None
Integrated into Swiss-Prot on January 10, 2006
Sequence was last modified on September 13, 2005 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 23)
Name and origin of the protein
Protein name Histidinol dehydrogenase
Synonyms HDH
EC 1.1.1.23
Gene name
Name: hisD
OrderedLocusNames: Daro_3387
From
Dechloromonas aromatica (strain RCB) [TaxID: 159087] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Rhodocyclaceae; Dechloromonas.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S., Kellar K., Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.;
"Complete sequence of Dechloromonas aromatica RCB.";
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CP000089; AAZ48116.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_286586.1; -.
3D structure databases
ModBase Q47AL5.
Enzyme and pathway databases
BioCyc DARO159087:DARO_3387-MON; -.
Ontologies
GO
GO:0004399; Molecular function: histidinol dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0000105; Biological process: histidine biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_01024; -; 1.
PBIL [Tree]
InterPro IPR001692; Histidinol_DHase.
IPR012131; Hstdl_DHase_prok.
IPR002035; VWF_A.
Graphical view of domain structure.
PANTHER PTHR21256:SF2; Hstdl_DH_prok; 1.
Pfam PF00815; Histidinol_dh; 1.
Pfam graphical view of domain structure.
PRINTS PR00083; HOLDHDRGNASE.
PR00453; VWFADOMAIN.
ProDom PD002680; Histidinol_dh; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00069; hisD; 1.
PROSITE PS00611; HISOL_DEHYDROGENASE; 1.
BLOCKS Q47AL5.
ProtoNet Q47AL5.
Genome annotation databases
GeneID 3567117; -.
GenomeReviews CP000089_GR; Daro_3387.
KEGG dar:Daro_3387; -.
NMPDR fig|159087.4.peg.3635; -.
Phylogenomic databases
HOGENOM Q47AL5; -.
Genome annotation databases
CMR Q47AL5; Daro_3387.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis; Metal-binding; NAD; Oxidoreductase; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   433  433     Histidinol dehydrogenase. PRO_0000135763
ACT_SITE   330   330        Proton acceptor (By similarity). 
ACT_SITE   331   331        Proton acceptor (By similarity). 
METAL   262   262        Zinc (By similarity). 
METAL   265   265        Zinc (By similarity). 
METAL   364   364        Zinc (By similarity). 
METAL   423   423        Zinc (By similarity). 
BINDING   133   133        NAD (By similarity). 
BINDING   194   194        NAD (By similarity). 
BINDING   217   217        NAD (By similarity). 
BINDING   240   240        Substrate (By similarity). 
BINDING   262   262        Substrate (By similarity). 
BINDING   265   265        Substrate (By similarity). 
BINDING   331   331        Substrate (By similarity). 
BINDING   364   364        Substrate (By similarity). 
BINDING   418   418        Substrate (By similarity). 
BINDING   423   423        Substrate (By similarity). 
Sequence information
Length: 433 AA [This is the length of the unprocessed precursor] Molecular weight: 46066 Da [This is the MW of the unprocessed precursor] CRC64: A7E2E5E5990A7CCA [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MVAIKRLATV DADFKAQMDA LLAFEAAQDE GIERTVIGIL ADVKARGDAA VVEYSNKFDR 

        70         80         90        100        110        120 
LTASSMADLE LSKAEMQKAL DGLPADQRQA LEAAAHRVRV YHEKQRMEGW SYTEADGTML 

       130        140        150        160        170        180 
GQMITPLDRV GLYVPGGKAA YPSSVLMNAI PAKVAGVKEL IMVVPTPGGE HNQLVLAAAC 

       190        200        210        220        230        240 
LAGVDRVFTI GGAQAVGALA YGTEAVPQVD KIVGPGNAYV ACAKRRVFGI VGIDMIAGPS 

       250        260        270        280        290        300 
EILVVADGSS DPDWVAMDLF SQAEHDELAQ SILICTDAAY IDRVQASIEK LLPTMPRREV 

       310        320        330        340        350        360 
IETSLTNRGA LILVRDLEEA CAIANRVAPE HLELSLADPD PWVAKIHHAG AIFIGHYTSE 

       370        380        390        400        410        420 
SLGDYCAGPN HVLPTSGSAR FSSPLGVYDF QKRTSLIKVS KAGAQTLGKI ASTLAHGEGL 

       430 
PAHAKSAEFR LEN
Q47AL5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!