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UniProtKB/Swiss-Prot entry Q88QC7

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

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Entry information
Entry name SPEA_PSEPK
Primary accession number Q88QC7
Secondary accession numbers None
Integrated into Swiss-Prot on March 29, 2004
Sequence was last modified on June 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 37)
Name and origin of the protein
Protein name Biosynthetic arginine decarboxylase
Synonyms ADC
EC 4.1.1.19
Gene name
Name: speA
OrderedLocusNames: PP_0567
From
Pseudomonas putida (strain KT2440) [TaxID: 160488] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1046/j.1462-2920.2002.00366.x; PubMed=12534463 [NCBI, ExPASy, EBI, Israel, Japan]
Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H., Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M., Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F., Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I., Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A., Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H., Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C., Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
"Complete genome sequence and comparative analysis of the metabolically versatile Pseudomonas putida KT2440.";
Environ. Microbiol. 4:799-808(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
AE015451; AAN66194.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_742730.1; -.
3D structure databases
ModBase Q88QC7.
Enzyme and pathway databases
BioCyc PPUT160488:PP_0567-MON; -.
Ontologies
GO
GO:0008792; Molecular function: arginine decarboxylase activity (inferred from electronic annotation from HAMAP).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006527; Biological process: arginine catabolic process (inferred from electronic annotation from InterPro).
GO:0008295; Biological process: spermidine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01417; -; 1.
PBIL [Tree]
InterPro IPR002985; Arg_decrbxlase.
IPR000183; De-COase2.
Graphical view of domain structure.
PANTHER PTHR11482:SF3; Arg_decrbxlase; 1.
Pfam PF02784; Orn_Arg_deC_N; 1.
PF00278; Orn_DAP_Arg_deC; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001336; Arg_decrbxlase; 1.
PRINTS PR01180; ARGDCRBXLASE.
PR01179; ODADCRBXLASE.
TIGRFAMs TIGR01273; speA; 1.
PROSITE PS00878; ODR_DC_2_1; FALSE_NEG.
PS00879; ODR_DC_2_2; 1.
BLOCKS Q88QC7.
ProtoNet Q88QC7.
Genome annotation databases
GeneID 1044357; -.
GenomeReviews AE015451_GR; PP_0567.
KEGG ppu:PP_0567; -.
NMPDR fig|160488.1.peg.560; -.
TIGR PP_0567; -.
Phylogenomic databases
HOGENOM Q88QC7; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Decarboxylase; Lyase; Magnesium; Metal-binding; Polyamine biosynthesis; Pyridoxal phosphate; Spermidine biosynthesis.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   637  637     Biosynthetic arginine decarboxylase. PRO_0000149972
REGION   290   300  11     Substrate-binding (Potential). 
BINDING   110   110        Pyridoxal phosphate (covalent) (By similarity). 
Sequence information
Length: 637 AA [This is the length of the unprocessed precursor] Molecular weight: 71043 Da [This is the MW of the unprocessed precursor] CRC64: E59F5EA60F345738 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSVRRTRKDD GSQWTVADSR SVYGIRHWGA GYFAINEAGR VEVRPNGPQS APIDLFEQVD 

        70         80         90        100        110        120 
ELRQSGLSLP LLVRFPDILQ DRVRQLTGAF DANIARLEYQ SQYTALYPIK VNQQEAVVEN 

       130        140        150        160        170        180 
IIATQNVSIG LEAGSKPELL AVLALAPKGG TIVCNGYKDR EFIRLALMGQ KLGHNVFIVI 

       190        200        210        220        230        240 
EKESEVALVI EEAAELKVKP QVGLRVRLSS LASSKWADTG GEKSKFGLSA AQLLSVVQRF 

       250        260        270        280        290        300 
RDAGLDQGIR LLHFHMGSQI ANLADYQHGF KEAIRYYGEL RALGLPVDHI DVGGGLGVDY 

       310        320        330        340        350        360 
DGTHSRNASS INYDMDDYAG VVVGMLKEFC DAQGLPHPHI FSESGRSLTA HHAMLVIQVT 

       370        380        390        400        410        420 
DVEKHNDDVP TIENKEALPE TVQWLVDLLG PTDIEMVTET YWRATHYMGD VAAQYADGKL 

       430        440        450        460        470        480 
SLGEKALAEQ CYFAVCRRLH NSLKARQRSH RQVLDELNDK LADKYICNFS VFQSLPDTWA 

       490        500        510        520        530        540 
IGQVLPIIPL HRLDEEPMRR AVLQDLTCDS DGKINQYVDE QSIETSMPVH AVKEGEDYLL 

       550        560        570        580        590        600 
GVFLVGAYQE ILGDMHNLFG DTDSVNIYQN ADGSVYHAGI ETHDTIEDML RYVHLSPEEL 

       610        620        630 
MTHYRDKVAS AKITARERTQ YLDALRLGLT RSSYLSS
Q88QC7 in FASTA format

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