Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A8FWJ3 (SPEA_SHESH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. 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:Ssed_2609
OrganismShewanella sediminis (strain HAW-EB3) [Complete proteome] [HAMAP]
Taxonomic identifier425104 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length637 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 – 637637Biosynthetic arginine decarboxylase HAMAP-Rule MF_01417
PRO_1000087409

Regions

Region286 – 29611Substrate-binding Potential

Amino acid modifications

Modified residue1011N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A8FWJ3 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: C7C03577B46A88ED

FASTA63771,200
        10         20         30         40         50         60 
MSDWSINDAR TGYNVNYWSQ GLYGISDTGE VTVSPDPSHP EYSIGLNELA KDMVKSGVAL 

        70         80         90        100        110        120 
PVLIRFPQIL HHRVNSVCQA FNQAIQKYEY QSDYLLVYPI KVNQQQTVVE EILASQVSKE 

       130        140        150        160        170        180 
VPQLGLEAGS KPELMAVLAM AQKASSVIIC NGYKDVEYIR LALIGEKLGH KVYIVLEKLS 

       190        200        210        220        230        240 
ELKIILEEAE KLGVTPRLGC RVRLAFQGKG KWQASGGEKS KFGLSASQVL TVIDSLKQSQ 

       250        260        270        280        290        300 
MLDSLQLLHF HLGSQIANIR DIRQGVSEAG RFYCELQKLG ANVKCFDVGG GLAVDYDGTR 

       310        320        330        340        350        360 
SQSSSSMNYG LTEYANNIVS VLTDLCNEYK EPMPRIISES GRFLTAHHAV LITDVIGTEA 

       370        380        390        400        410        420 
YKPEVIEEPE TEAPQLLHNM WQSWSEVSGR ADQRALIEIY HDCQSDLSEV HSLFALGQLS 

       430        440        450        460        470        480 
LSERAWAEQV NLRVCHELRD VMSPKYRFHR PIIDELNEKL ADKFFVNFSL FQSLPDAWGI 

       490        500        510        520        530        540 
DQVFPIMPLS GLDKAPERRA VMLDITCDSD GTIDQYVDGQ GIETTIPVPT WSAESPYLIG 

       550        560        570        580        590        600 
FFLVGAYQEI LGDMHNLFGD TNSAVVRLDD DGRTNIESVL AGDTVADVLR YVNLDAVSFM 

       610        620        630 
RTYEELVNKH IQEAERANIL EELQLGLKGY TYLEDFS 

« Hide

References

[1]"Complete sequence of Shewanella sediminis HAW-EB3."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Zhao J.-S., Richardson P.
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HAW-EB3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000821 Genomic DNA. Translation: ABV37216.1.
RefSeqYP_001474344.1. NC_009831.1.

3D structure databases

ProteinModelPortalA8FWJ3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING425104.Ssed_2609.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV37216; ABV37216; Ssed_2609.
GeneID5610937.
KEGGsse:Ssed_2609.
PATRIC23562887. VBISheSed62411_2782.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSSED425104:GH7Q-2707-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.
SUPFAMSSF50621. SSF50621. 1 hit.
TIGRFAMsTIGR01273. speA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSPEA_SHESH
AccessionPrimary (citable) accession number: A8FWJ3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 13, 2007
Last modified: February 19, 2014
This is version 48 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