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UniProtKB/Swiss-Prot entry Q3ACY8


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

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Entry information
Entry name DAPB_CARHZ
Primary accession number Q3ACY8
Secondary accession numbers None
Integrated into Swiss-Prot on March 21, 2006
Sequence was last modified on November 22, 2005 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 21)
Name and origin of the protein
Protein name Dihydrodipicolinate reductase
Synonyms DHPR
EC 1.3.1.26
Gene name
Name: dapB
OrderedLocusNames: CHY_1151
From
Carboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008) [TaxID: 246194] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; Thermoanaerobacteraceae; Carboxydothermus.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1371/journal.pgen.0010065; PubMed=16311624 [NCBI, ExPASy, EBI, Israel, Japan]
Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J., Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J., Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
"Life in hot carbon monoxide: the complete genome sequence of Carboxydothermus hydrogenoformans Z-2901.";
PLoS Genet. 1:563-574(2005).
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
CP000141; ABB15299.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_359996.1; -.
3D structure databases
ModBase Q3ACY8.
Enzyme and pathway databases
BioCyc CHYD246194:CHY_1151-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0008839; Molecular function: dihydrodipicolinate reductase activity (inferred from electronic annotation from HAMAP).
GO:0019877; Biological process: diaminopimelate biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00102; -; 1.
PBIL [Tree]
InterPro IPR000846; DapB.
IPR011770; DapB_bac/pln.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR20836; DapB_bac/pln; 1.
Pfam PF05173; DapB_C; 1.
PF01113; DapB_N; 1.
Pfam graphical view of domain structure.
ProDom PD004105; DapB; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00036; dapB; 1.
PROSITE PS01298; DAPB; 1.
BLOCKS Q3ACY8.
Genome annotation databases
GeneID 3727402; -.
GenomeReviews CP000141_GR; CHY_1151.
KEGG chy:CHY_1151; -.
NMPDR fig|246194.3.peg.1197; -.
TIGR CHY_1151; -.
Phylogenomic databases
HOGENOM Q3ACY8; -.
Other
ProtoNet Q3ACY8.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Cytoplasm; Diaminopimelate biosynthesis; Lysine biosynthesis; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   263  263     Dihydrodipicolinate reductase. PRO_0000228336
Sequence information
Length: 263 AA [This is the length of the unprocessed precursor] Molecular weight: 28959 Da [This is the MW of the unprocessed precursor] CRC64: AED778FBC2090F33 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MARIVMLGAC GKMGREISKN LLMHSEHELV GFVDVVNVGQ DFGEILGISR LGKTVEDNLK 

        70         80         90        100        110        120 
EVILKTNPEI VLDFSRASGA FTNILIALEN KVRVVSGTTG FSQEQIKKIE DVSNANNLGC 

       130        140        150        160        170        180 
IIAPNFSIGA LLLMKLAQMA AKYFSHVEII EYHHNLKVDA PSGTAIKTAE LLSSIRENQP 

       190        200        210        220        230        240 
SAIQEEEKIP GSRGGDYRGI KIHSVRLPGL VAHQEVIFGG RGQSLTLRHD VYSRESYLDG 

       250        260 
ILFALKKVLE LDRFVFGLDE LLF 

Q3ACY8 in FASTA format

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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

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