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UniProtKB/Swiss-Prot entry A9N512


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

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Entry information
Entry name ULAD_SALPB
Primary accession number A9N512
Secondary accession numbers None
Integrated into Swiss-Prot on May 20, 2008
Sequence was last modified on February 5, 2008 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 8)
Name and origin of the protein
Protein name 3-keto-L-gulonate-6-phosphate decarboxylase ulaD
Synonyms EC 4.1.1.85
3-dehydro-L-gulonate-6-phosphate decarboxylase
KGPDC
L-ascorbate utilization protein D
Gene name
Name: ulaD
OrderedLocusNames: SPAB_05520
From
Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7) [TaxID: 272994] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Salmonella; Salmonella enterica subsp. enterica serovar Paratyphi B.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R.;
Submitted (NOV-2007) 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
CP000886; ABX70789.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001591622.1; -.
3D structure databases
ModBase A9N512.
Ontologies
GO
GO:0033982; Molecular function: 3-dehydro-L-gulonate-6-phosphate decarboxylase activity (inferred from electronic annotation from EC).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005975; Biological process: carbohydrate metabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0019854; Biological process: L-ascorbic acid catabolic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01267; -; 1.
PBIL [Tree]
InterPro IPR013785; Aldolase_TIM.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
Genome annotation databases
GeneID 5779128; -.
GenomeReviews CP000886_GR; SPAB_05520.
KEGG spq:SPAB_05520; -.
CMR A9N512; SPAB_05520.
Other
ProtoNet A9N512.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Carbohydrate metabolism; Complete proteome; Decarboxylase; Lyase; Magnesium; Metal-binding.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   216  216     3-keto-L-gulonate-6-phosphate decarboxylase ulaD. PRO_1000085827
METAL   33    33        Magnesium (By similarity). 
METAL   62    62        Magnesium (By similarity). 
BINDING   11    11        Substrate (By similarity). 
BINDING   192   192        Substrate (By similarity). 
SITE   64    64  1     Transition state stabilizer (By similarity). 
SITE   67    67  1     Transition state stabilizer (By similarity). 
Sequence information
Length: 216 AA [This is the length of the unprocessed precursor] Molecular weight: 23706 Da [This is the MW of the unprocessed precursor] CRC64: CDF280DC1D1BAD68 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSLPMLQVAL DNQTMDSAYE TTRLIAEEVD IIEVGTILCV GEGVRAVRDL KALYPHKIVL 

        70         80         90        100        110        120 
ADAKIADAGK ILSRMCFEAN ADWVTVICCA DINTAKGALD VAKEFNGDVQ IELTGYWTWE 

       130        140        150        160        170        180 
QAQQWRDAGI QQVVYHRSRD AQAAGVAWGE ADITAIKRLS DMGFKVTVTG GLALEDLPLF 

       190        200        210 
KGIPIHVFIA GRSIRDAESP VEAARQFKRS IAQLWG 

A9N512 in FASTA format

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