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

A6WM65 (SPEA_SHEB8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. 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:Shew185_1761
OrganismShewanella baltica (strain OS185) [Complete proteome] [HAMAP]
Taxonomic identifier402882 [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_1000024266

Regions

Region286 – 29611Substrate-binding Potential

Amino acid modifications

Modified residue1011N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A6WM65 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: ADF1EB11628530BF

FASTA63770,894
        10         20         30         40         50         60 
MNDWSIDDAR AGYNVTHWSQ GFYGISDHGE VTVSPDPKNP DYKIGLNELA KDMVKAGVAL 

        70         80         90        100        110        120 
PVLVRFPQIL HHRVNSLCQA FDQAIQKYEY QADYLLVYPI KVNQQQTVVE EILASQASKE 

       130        140        150        160        170        180 
VPQLGLEAGS KPELMAVLAM AQKASSVIVC NGYKDNEYIR LALIGEKLGH KVYIVLEKLS 

       190        200        210        220        230        240 
ELKMVLAESK RLGVTPRLGL RARLAFQGKG KWQASGGEKS KFGLSAAQIL LVVEQLKQND 

       250        260        270        280        290        300 
MLDSLQLLHF HLGSQIANIR DIRQGVSEAG RFYCELRALG ASVNCFDVGG GLAVDYDGTR 

       310        320        330        340        350        360 
SQSNNSMNYG LTEYANNIVN VLTDICNEYE QPMPRIISES GRYLTAHHAV LITDVIGTEA 

       370        380        390        400        410        420 
YQPEDIQPPA EESPQLLHNM WHSWSELSGR ADQRALIEIY HDSQSDLQEA HSLFALGQLS 

       430        440        450        460        470        480 
LAERAWAEQA NLRVCHEVQG LLSAKNRYHR PIIDELNEKL ADKFFVNFSL FQSLPDAWGI 

       490        500        510        520        530        540 
DQVFPVLPLS GLDKAPERRA VMLDITCDSD GIVDQYVDGQ GIETTLPVPA WSADSPYLIG 

       550        560        570        580        590        600 
FFLVGAYQEI LGDMHNLFGD TNSAVVRIED NGVTNIESVL AGDTVADVLR YVNLDAVAFM 

       610        620        630 
RTYEELVNLH IAEDERAQIL EELQVGLKGY TYLEDFS 

« Hide

References

[1]"Complete sequence of chromosome of Shewanella baltica OS185."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Mikhailova N., Brettar I., Rodrigues J., Konstantinidis K., Tiedje J., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OS185.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000753 Genomic DNA. Translation: ABS07904.1.
RefSeqYP_001365967.1. NC_009665.1.

3D structure databases

ProteinModelPortalA6WM65.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING402882.Shew185_1761.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS07904; ABS07904; Shew185_1761.
GeneID5371239.
KEGGsbm:Shew185_1761.
PATRIC23460244. VBISheBal127872_1942.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSBAL402882:GJ99-1808-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_SHEB8
AccessionPrimary (citable) accession number: A6WM65
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: February 19, 2014
This is version 47 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