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UniProtKB/Swiss-Prot entry Q5LL27

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

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Entry information
Entry name HISX3_SILPO
Primary accession number Q5LL27
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 27)
Name and origin of the protein
Protein name Histidinol dehydrogenase 3
Synonyms HDH 3
EC 1.1.1.23
Gene name
Name: hisD3
OrderedLocusNames: SPOA0202
From
Silicibacter pomeroyi [TaxID: 89184] [HAMAP proteome]
Encoded on Plasmid megaplasmid Spo.
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
CP000032; AAV97336.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_165031.1; -.
3D structure databases
ModBase Q5LL27.
Enzyme and pathway databases
BioCyc SPOM246200:SPO_A0202-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 Q5LL27.
Genome annotation databases
GeneID 3196717; -.
GenomeReviews CP000032_GR; SPOA0202.
KEGG sil:SPOA0202; -.
NMPDR fig|246200.3.peg.68; -.
Phylogenomic databases
HOGENOM Q5LL27; -.
Genome annotation databases
CMR Q5LL27; SPOA0202.
Other
ProtoNet Q5LL27.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis; Metal-binding; NAD; Oxidoreductase; Plasmid; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   433  433     Histidinol dehydrogenase 3. PRO_0000135848
ACT_SITE   327   327        Proton acceptor (By similarity). 
ACT_SITE   328   328        Proton acceptor (By similarity). 
METAL   259   259        Zinc (By similarity). 
METAL   262   262        Zinc (By similarity). 
METAL   361   361        Zinc (By similarity). 
METAL   420   420        Zinc (By similarity). 
BINDING   130   130        NAD (By similarity). 
BINDING   191   191        NAD (By similarity). 
BINDING   214   214        NAD (By similarity). 
BINDING   237   237        Substrate (By similarity). 
BINDING   259   259        Substrate (By similarity). 
BINDING   262   262        Substrate (By similarity). 
BINDING   328   328        Substrate (By similarity). 
BINDING   361   361        Substrate (By similarity). 
BINDING   415   415        Substrate (By similarity). 
BINDING   420   420        Substrate (By similarity). 
Sequence information
Length: 433 AA [This is the length of the unprocessed precursor] Molecular weight: 45887 Da [This is the MW of the unprocessed precursor] CRC64: C15B11CCF2ACC563 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MPQFLDSRQP DFETAFTALL GAKREDSPDV DAVVAGIIAD VRARGDAAVI ELTERFDRVA 

        70         80         90        100        110        120 
LTPQSLRFST EEIAQAVDEV PAPERAALEL AAARIRAYHE RQMPQDADWT DDTGARLGWR 

       130        140        150        160        170        180 
WSAVSAAGLY VPGGLASYPS SVLMNAIPAK VAGVGRLAIA VPTPDGQVNP LVLLAAQISG 

       190        200        210        220        230        240 
VDEVYRIGGA QAIAALAYGT DTIAPVDKIT GPGNAFVAAA KRRVFGKVGI DMIAGPSEIL 

       250        260        270        280        290        300 
VIADRDNDPD WIALDLLSQA EHDESAQSIL ITDDAAFGRA VAEAVDKRLE TLERRAIAGV 

       310        320        330        340        350        360 
SWRDFGAVIT VSDLDEAAAL SNRIAPEHLE LCVSDPEALA ARTIHAGAIF LGQYTPEAIG 

       370        380        390        400        410        420 
DYVGGPNHVL PTARSARFSS GLSVMDFLKR TTMSRMTPEA LRAIGPAAAQ LARSESLEAH 

       430 
GLSVQARLDR LNG
Q5LL27 in FASTA format

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