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UniProtKB/Swiss-Prot entry Q3MEV7

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

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Entry information
Entry name HISX1_ANAVT
Primary accession number Q3MEV7
Secondary accession numbers None
Integrated into Swiss-Prot on April 4, 2006
Sequence was last modified on October 25, 2005 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 22)
Name and origin of the protein
Protein name Histidinol dehydrogenase 1
Synonyms HDH 1
EC 1.1.1.23
Gene name
Name: hisD1
OrderedLocusNames: Ava_0855
From
Anabaena variabilis (strain ATCC 29413 / PCC 7937) [TaxID: 240292] [HAMAP proteome]
Taxonomy Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
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., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
"Complete sequence of Anabaena variabilis ATCC 29413.";
Submitted (SEP-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
CP000117; ABA20479.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_321374.1; -.
3D structure databases
ModBase Q3MEV7.
Enzyme and pathway databases
BioCyc AVAR240292:AVA_0855-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.
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 Q3MEV7.
ProtoNet Q3MEV7.
Genome annotation databases
GeneID 3681756; -.
GenomeReviews CP000117_GR; Ava_0855.
KEGG ava:Ava_0855; -.
NMPDR fig|240292.3.peg.61; -.
Phylogenomic databases
HOGENOM Q3MEV7; -.
Genome annotation databases
CMR Q3MEV7; Ava_0855.
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   431  431     Histidinol dehydrogenase 1. PRO_0000229848
ACT_SITE   324   324        Proton acceptor (By similarity). 
ACT_SITE   325   325        Proton acceptor (By similarity). 
METAL   256   256        Zinc (By similarity). 
METAL   259   259        Zinc (By similarity). 
METAL   358   358        Zinc (By similarity). 
METAL   417   417        Zinc (By similarity). 
BINDING   127   127        NAD (By similarity). 
BINDING   188   188        NAD (By similarity). 
BINDING   211   211        NAD (By similarity). 
BINDING   234   234        Substrate (By similarity). 
BINDING   256   256        Substrate (By similarity). 
BINDING   259   259        Substrate (By similarity). 
BINDING   325   325        Substrate (By similarity). 
BINDING   358   358        Substrate (By similarity). 
BINDING   412   412        Substrate (By similarity). 
BINDING   417   417        Substrate (By similarity). 
Sequence information
Length: 431 AA [This is the length of the unprocessed precursor] Molecular weight: 45806 Da [This is the MW of the unprocessed precursor] CRC64: D3AC6AF531ED1B1A [This is a checksum on the sequence] 
        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
Q3MEV7 in FASTA format

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