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 Q8CX61

[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 DHA_OCEIH
Primary accession number Q8CX61
Secondary accession numbers None
Integrated into Swiss-Prot on August 16, 2004
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 34)
Name and origin of the protein
Protein name Alanine dehydrogenase
Synonym EC 1.4.1.1
Gene name
Name: ald
OrderedLocusNames: OB3225
From
Oceanobacillus iheyensis [TaxID: 182710] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Oceanobacillus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 14371 / JCM 11309 / KCTC 3954 / HTE831;
DOI=10.1093/nar/gkf526; PubMed=12235376 [NCBI, ExPASy, EBI, Israel, Japan]
Takami H., Takaki Y., Uchiyama I.;
"Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge and its unexpected adaptive capabilities to extreme environments.";
Nucleic Acids Res. 30:3927-3935(2002).
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
BA000028; BAC15181.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_694147.1; -.
3D structure databases
HSSP O52942; 1SAY. [HSSP ENTRY / PDB]
ModBase Q8CX61.
Enzyme and pathway databases
BioCyc OIHE221109:OB3225-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0000286; Molecular function: alanine dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0030435; Biological process: sporulation resulting in formation of a cellular spore (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR007698; Ala_DHase/PNT_C.
IPR008142; Ala_DHase/PNT_CS1.
IPR008143; Ala_DHase/PNT_CS2.
IPR007886; Ala_DHase/PNT_N.
IPR008141; Ala_DHase_PNT.
Graphical view of domain structure.
Pfam PF01262; AlaDh_PNT_C; 1.
PF05222; AlaDh_PNT_N; 1.
Pfam graphical view of domain structure.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00518; alaDH; 1.
PROSITE PS00836; ALADH_PNT_1; 1.
PS00837; ALADH_PNT_2; 1.
Genome annotation databases
GeneID 1016523; -.
GenomeReviews BA000028_GR; OB3225.
KEGG oih:OB3225; -.
NMPDR fig|221109.1.peg.3227; -.
Phylogenomic databases
HOGENOM Q8CX61; -.
Genome annotation databases
CMR Q8CX61; OB3225.
Other
ProtoNet Q8CX61.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; NAD; Oxidoreductase; Sporulation.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   376  376     Alanine dehydrogenase. PRO_0000198993
NP_BIND   169   199  31     NAD (By similarity). 
ACT_SITE   96    96        Potential. 
Sequence information
Length: 376 AA [This is the length of the unprocessed precursor] Molecular weight: 39619 Da [This is the MW of the unprocessed precursor] CRC64: EAC9F969A2041BC0 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MIIGVPKEIK NNENRVAMTP AGVVHLINAG HTVQIEKGAG LGSNFADAEY KEAGAELIDS 

        70         80         90        100        110        120 
AASVWENADM IMKVKEPLSS EYKYFRKGLI LFTYLHLAAA PELTKALVDS EVTAIAYETI 

       130        140        150        160        170        180 
TVNGTLPLLT PMSEVAGRMA TQIGAQYLEK SEGGKGILLG GIPGVSRGKV TVIGGGVVGT 

       190        200        210        220        230        240 
HAAKIALGLG AEVTIIDLNP VRLRQLDDIF GSSIQTLMSN PYNIAEAVKD SDLVIGSVLI 

       250        260        270        280        290        300 
PGRKAPKLVT DEMIQSMQPG SVLVDVAIDQ GGNFETVDHP TTHDEPIYVK HDVLHYAVAN 

       310        320        330        340        350        360 
IPGAVPRTAT VGLTNVTVPY AVQIASKGAV KAIQDNPAIL TGVNVMNGKV TYEAVAADLG 

       370 
YDFVSPEDAI KDAELV
Q8CX61 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 ca flag CBR Canada Mirror sites: Australia Brazil China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!