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UniProtKB/Swiss-Prot entry Q12LW6


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

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Entry information
Entry name SPEA_SHEDO
Primary accession number Q12LW6
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on August 22, 2006 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 24)
Name and origin of the protein
Protein name Biosynthetic arginine decarboxylase
Synonyms ADC
EC 4.1.1.19
Gene name
Name: speA
OrderedLocusNames: Sden_2280
From
Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013) [TaxID: 318161] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; Shewanellaceae; Shewanella.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
"Complete sequence of Shewanella denitrificans OS217.";
Submitted (MAR-2006) 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
CP000302; ABE55560.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_563283.1; -.
3D structure databases
ModBase Q12LW6.
Enzyme and pathway databases
BioCyc SDEN318161:SDEN_2280-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; FALSE_NEG.
ProtoNet Q12LW6.
Genome annotation databases
GeneID 4018772; -.
GenomeReviews CP000302_GR; Sden_2280.
KEGG sdn:Sden_2280; -.
NMPDR fig|318161.14.peg.2221; -.
Phylogenomic databases
HOGENOM Q12LW6; -.
Genome annotation databases
CMR Q12LW6; Sden_2280.
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   636  636     Biosynthetic arginine decarboxylase. PRO_1000024267
REGION   286   296  11     Substrate-binding (Potential). 
BINDING   101   101        Pyridoxal phosphate (covalent) (By similarity). 
Sequence information
Length: 636 AA [This is the length of the unprocessed precursor] Molecular weight: 71065 Da [This is the MW of the unprocessed precursor] CRC64: 67F1E19B36DD55CA [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNDWTIEDAR AGYNVTHWSQ GFYGIGEAGE VTVSPDPLNP SNKVALDTLA QDLVQAGIAL 

        70         80         90        100        110        120 
PVLVRFPQIL HHRVESLCDA FNQAIQKYEY QNDYLLVYPI KVNQQKTVVE EILASQVSKE 

       130        140        150        160        170        180 
VPQLGLEAGS KPELMAVLAM AQKASSVIVC NGYKDKEYVR LALIGEKLGH KVYIVLEKMS 

       190        200        210        220        230        240 
ELKMVLEEAR ELGVTPRLGL RTRLAFQGKG KWQASGGEKS KFGLSAAQVL KVVDELKEAN 

       250        260        270        280        290        300 
MLESLQLLHF HLGSQIANIR DIRQGVSEAG RFYCELRQLG ASINCFDVGG GLAVDYDGTR 

       310        320        330        340        350        360 
SQSNNSMNYG LTEYANNIVN VLTDLCNEYE QPMPRIISES GRHLTAHHAV LITDVIGTEA 

       370        380        390        400        410        420 
YMPENIQAPA EDAPQLLHNM WQSWTEISGR HDQRAIIEIY HDSQSDIAEA HSLFAVGQLS 

       430        440        450        460        470        480 
LMDRAWAEQT NLRVCHEVKG LLSNNNRYHR PVIDELNEKL ADKLFVNFSL FQSLPDAWGI 

       490        500        510        520        530        540 
DQVFPVLPLT CLDKAPERRA VMLDITCDSD GIVDQYVDGQ GIETTLPVPA WDPANPYLIG 

       550        560        570        580        590        600 
FFMVGAYQEI LGDMHNLFGD TNSAVVFVED NGKARIESTL DGDTVADVLR YVNLDADEFM 

       610        620        630 
HTYEELVEQH IVEDERASIL EELQLGLKGY TYLEDF 

Q12LW6 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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NPSA logo NPSA Sequence analysis tools

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