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Q12LW6 (SPEA_SHEDO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Biosynthetic arginine decarboxylase

Short name=ADC
EC=4.1.1.19
Gene names
Name:speA
Ordered Locus Names:Sden_2280
OrganismShewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013) [Complete proteome] [HAMAP]
Taxonomic identifier318161 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length636 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the biosynthesis of agmatine from arginine By similarity. HAMAP-Rule MF_01417

Catalytic activity

L-arginine = agmatine + CO2. HAMAP-Rule MF_01417

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01417

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01417

Pathway

Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1. HAMAP-Rule MF_01417

Sequence similarities

Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 636636Biosynthetic arginine decarboxylase HAMAP-Rule MF_01417
PRO_1000024267

Regions

Region286 – 29611Substrate-binding Potential

Amino acid modifications

Modified residue1011N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q12LW6 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 67F1E19B36DD55CA

FASTA63671,065
        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 

« Hide

References

[1]"Complete sequence of Shewanella denitrificans OS217."
US DOE Joint Genome Institute
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. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OS217 / ATCC BAA-1090 / DSM 15013.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000302 Genomic DNA. Translation: ABE55560.1.
RefSeqYP_563283.1. NC_007954.1.

3D structure databases

ProteinModelPortalQ12LW6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING318161.Sden_2280.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE55560; ABE55560; Sden_2280.
GeneID4018772.
KEGGsdn:Sden_2280.
PATRIC23490479. VBISheDen79529_2399.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1166.
HOGENOMHOG000029191.
KOK01585.
OMAMIHFHIG.
OrthoDBEOG676Z0R.
ProtClustDBPRK05354.

Enzyme and pathway databases

BioCycSDEN318161:GHKQ-2356-MONOMER.
UniPathwayUPA00186; UER00284.

Family and domain databases

Gene3D2.40.37.10. 2 hits.
HAMAPMF_01417. SpeA.
InterProIPR009006. Ala_racemase/Decarboxylase_C.
IPR002985. Arg_decrbxlase.
IPR022643. De-COase2_C.
IPR022644. De-COase2_N.
IPR000183. Orn/DAP/Arg_de-COase.
[Graphical view]
PfamPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PIRSFPIRSF001336. Arg_decrbxlase. 1 hit.
PRINTSPR01180. ARGDCRBXLASE.
PR01179. ODADCRBXLASE.
TIGRFAMsTIGR01273. speA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSPEA_SHEDO
AccessionPrimary (citable) accession number: Q12LW6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 22, 2006
Last modified: February 19, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways