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 Q989E7


[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 HISX1_RHILO
Primary accession number Q989E7
Secondary accession numbers None
Integrated into Swiss-Prot on March 25, 2003
Sequence was last modified on October 1, 2001 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 39)
Name and origin of the protein
Protein name Histidinol dehydrogenase 1
Synonyms HDH 1
EC 1.1.1.23
Gene name
Name: hisD1
OrderedLocusNames: mll6456
From
Rhizobium loti (Mesorhizobium loti) [TaxID: 381] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Phyllobacteriaceae; Mesorhizobium.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MAFF303099;
DOI=10.1093/dnares/7.6.331; PubMed=11214968 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.;
"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti.";
DNA Res. 7:331-338(2000).
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
BA000012; BAB52750.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_106964.1; -.
3D structure databases
HSSP P06988; 1K75. [HSSP ENTRY / PDB]
ModBase Q989E7.
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 Q989E7.
Genome annotation databases
GeneID 1229619; -.
GenomeReviews BA000012_GR; mll6456.
KEGG mlo:mll6456; -.
NMPDR fig|266835.1.peg.5065; -.
Phylogenomic databases
HOGENOM Q989E7; -.
Genome annotation databases
CMR Q989E7; mll6456.
Other
ProtoNet Q989E7.
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   430  430     Histidinol dehydrogenase 1. PRO_0000135829
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   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: 430 AA [This is the length of the unprocessed precursor] Molecular weight: 45685 Da [This is the MW of the unprocessed precursor] CRC64: 4B21C2FAAFB9E532 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAITLRQSDA DFEQRFAAFL TTKREVSEDV DAGVRQIIAR VRAEGDAALI DYTQRFDRAD 

        70         80         90        100        110        120 
LKSLGIAVSK QDIAAAYETA DPKAIEALEF ARDRIRSHHE RQRPKDDRYT DATGVELGWR 

       130        140        150        160        170        180 
WTAIEAVGLY VPGGTASYPS SVLMNAVPAR VAGVERVVMV VPAPGGIINP LVLVAADISG 

       190        200        210        220        230        240 
VTEIYRVGGA HAIAALAYGT ETIKPVAKIV GPGNAYVAAA KRQVFGTVGI DMIAGPSEVL 

       250        260        270        280        290        300 
VVADGSNNAD WIAADLLAQA EHDVSAQSIL ITDDPAFGKA VEQAVERQLQ TLPRGETAAA 

       310        320        330        340        350        360 
SWRDFGAVIE VATIEAALPL VDRIAAEHVE LAIDDAEGFL SRMRNAGAVF LGRHTPEAIG 

       370        380        390        400        410        420 
DYVGGSNHVL PTARSARFSS GLSVLDFVKR TSILKLGPEQ LRVLAPAAIA LAKAEGLDAH 

       430 
GRSVAIRLNM 

Q989E7 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 kr flag YPRC Korea Mirror sites: Australia  Brazil  Canada  China  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!