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Q083L6 (SPEA_SHEFN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Biosynthetic arginine decarboxylase

Short name=ADC
EC=4.1.1.19
Gene names
Name:speA
Ordered Locus Names:Sfri_1698
OrganismShewanella frigidimarina (strain NCIMB 400) [Complete proteome] [HAMAP]
Taxonomic identifier318167 [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_1000024268

Regions

Region286 – 29611Substrate-binding Potential

Amino acid modifications

Modified residue1011N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q083L6 [UniParc].

Last modified October 31, 2006. Version 1.
Checksum: C65C6E938E4E9116

FASTA63671,191
        10         20         30         40         50         60 
MSDWSIEDAR SGYNVTHWSQ GFYGIREDGE VTVSPNPQNP DHKVGLNELA KSMVEAGVSL 

        70         80         90        100        110        120 
PVLVRFPQIL HHRVESLCEA FNDAIKKYDY QNDYLLVYPI KVNQQKTVVE EILASQKSKE 

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

       190        200        210        220        230        240 
ELKMVLIEAE KLGITPRLGL RVRLAFQGKG KWQASGGEKS KFGLSAAQVL KVIAELKSAN 

       250        260        270        280        290        300 
MLDSLQLLHF HLGSQIANIR DIRQGVSEAG RFYCELRQLG ASIDCFDVGG GLAVDYDGTR 

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

       370        380        390        400        410        420 
YQPENIQEPS EDAPQLLHNM WQSWLEISGR YDQRAIIEIY HDSQSDISEA HSLFAVGQLS 

       430        440        450        460        470        480 
LADRAWAEQA NLRVCHEVKG LLSNNNRYHR PVIDELNEKL ADKFFVNFSL FQSLPDAWGI 

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

       550        560        570        580        590        600 
FFMVGAYQEI LGDMHNLFGD TNSAVVRIDE RGLSQIESVL EGDTVADVLR YVNLDAVDFM 

       610        620        630 
RTYEELVNQH IVEEERASIL EELQLGLKGY TYLEDF 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000447 Genomic DNA. Translation: ABI71549.1.
RefSeqYP_750387.1. NC_008345.1.

3D structure databases

ProteinModelPortalQ083L6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING318167.Sfri_1698.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI71549; ABI71549; Sfri_1698.
GeneID4277724.
KEGGsfr:Sfri_1698.
PATRIC23497347. VBISheFri14343_1761.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSFRI318167:GIXS-1763-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_SHEFN
AccessionPrimary (citable) accession number: Q083L6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 31, 2006
Last modified: February 19, 2014
This is version 54 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