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UniProtKB/Swiss-Prot entry Q5LUS2

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

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Entry information
Entry name HISX2_SILPO
Primary accession number Q5LUS2
Secondary accession numbers None
Integrated into Swiss-Prot on January 10, 2006
Sequence was last modified on February 1, 2005 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 29)
Name and origin of the protein
Protein name Histidinol dehydrogenase 2
Synonyms HDH 2
EC 1.1.1.23
Gene name
Name: hisD2
OrderedLocusNames: SPO0981
From
Silicibacter pomeroyi [TaxID: 89184] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; Rhodobacteraceae; Silicibacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
DOI=10.1038/nature03170; PubMed=15602564 [NCBI, ExPASy, EBI, Israel, Japan]
Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B., Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
"Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine environment.";
Nature 432:910-913(2004).
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
CP000031; AAV94285.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_166233.1; -.
3D structure databases
ModBase Q5LUS2.
Enzyme and pathway databases
BioCyc SPOM246200:SPO_0981-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).
QuickGo view.
Family and domain databases
HAMAP MF_01024; -; 1.
PBIL [Tree]
InterPro IPR001692; Histidinol_DHase.
IPR012131; Hstdl_DHase_prok.
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.
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 Q5LUS2.
Genome annotation databases
GeneID 3193830; -.
GenomeReviews CP000031_GR; SPO0981.
KEGG sil:SPO0981; -.
NMPDR fig|246200.3.peg.1401; -.
Phylogenomic databases
HOGENOM Q5LUS2; -.
Genome annotation databases
CMR Q5LUS2; SPO0981.
Other
ProtoNet Q5LUS2.
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 2. PRO_0000135847
ACT_SITE   319   319        Proton acceptor (By similarity). 
ACT_SITE   320   320        Proton acceptor (By similarity). 
METAL   249   249        Zinc (By similarity). 
METAL   252   252        Zinc (By similarity). 
METAL   353   353        Zinc (By similarity). 
METAL   412   412        Zinc (By similarity). 
BINDING   119   119        NAD (By similarity). 
BINDING   181   181        NAD (By similarity). 
BINDING   204   204        NAD (By similarity). 
BINDING   227   227        Substrate (By similarity). 
BINDING   249   249        Substrate (By similarity). 
BINDING   252   252        Substrate (By similarity). 
BINDING   320   320        Substrate (By similarity). 
BINDING   353   353        Substrate (By similarity). 
BINDING   407   407        Substrate (By similarity). 
BINDING   412   412        Substrate (By similarity). 
Sequence information
Length: 433 AA [This is the length of the unprocessed precursor] Molecular weight: 45353 Da [This is the MW of the unprocessed precursor] CRC64: B67DC5531FADA3A3 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTITVLKSAP GLPPAPQGDA ADVVQVMLAR LRAEGEAAAR DYAARLDGWS GEIVVSPDQV 

        70         80         90        100        110        120 
ARASEQVPED LKTQIRYAHD NIRRFAEAQR ASALDFQTEL RPGLIAGQKQ IPLAAAGAYV 

       130        140        150        160        170        180 
PGGRYAHIAS ALMSIATARA AGVGQITAVS PPQVGRGVHP AILYAMSLAG ADRILALGGV 

       190        200        210        220        230        240 
QGVAALAFGL FGAPPADILV GPGNQFVAEA KRQLFGPVGI DMFAGPTDSL VIADSTADPL 

       250        260        270        280        290        300 
TVAWDLVGQA EHGYNSPVWL VTDSAALAEA VLAHIPGCIA DLPEPNRSSA QAAWDALGEV 

       310        320        330        340        350        360 
ILCTDREEMA ATADRYAPEH LHVQAADLDW WRGRLSAYGS LFLGELTTVA FGDKASGPNH 

       370        380        390        400        410        420 
VLPTSGAARY TGGLSVHKFL KTVTWQQVAP QALPDLARAT ATISRAEGME GHARTADIRL 

       430 
EKLRPTLRQV GTG
Q5LUS2 in FASTA format

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