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Q9CL60 (SPEA_PASMU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:PM1382
OrganismPasteurella multocida (strain Pm70) [Complete proteome] [HAMAP]
Taxonomic identifier272843 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella

Protein attributes

Sequence length644 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

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 – 644644Biosynthetic arginine decarboxylase HAMAP-Rule MF_01417
PRO_0000149966

Regions

Region293 – 30311Substrate-binding Potential

Amino acid modifications

Modified residue1131N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CL60 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: F6A7FEB0B8DE3D82

FASTA64472,707
        10         20         30         40         50         60 
MEQVTLTSDG TSSVFAENTV REVCNINYWG MRYYNVDEKG DIFVCPDPDK PQNRVSLAAL 

        70         80         90        100        110        120 
AEKVQREQGA HLPTLFCFPQ IIQHRLRSIN QAFKRAREDF GYEGNYFLVY PIKVNQHRRI 

       130        140        150        160        170        180 
VESLISSGQP LGLEAGSKAE LMAVLAHAGI TQTVIVCNGY KDREYVRFAL MGEKLGHKVY 

       190        200        210        220        230        240 
LVIEKLSEIQ LVLEEAAKLN VKPRLGVRAR LASQGSGKWQ SSGGEKSKFG LSASQVLSLV 

       250        260        270        280        290        300 
QMLKEHECLD CLQLLHFHLG SQLGNIRDVA TGVRESARFY VELHKLGVNI QCFDVGGGLG 

       310        320        330        340        350        360 
VDYEGNRTQS DCSVNYGLNE YADTVVWGIG QACREHGLPH PTIITESGRG VTAHHAVLVS 

       370        380        390        400        410        420 
NVIGVERYKF ETLAAPAKDA PSVLHSMWET WVDIQSSREK RSLRSWIHES QFDLSDVHNQ 

       430        440        450        460        470        480 
YNVGLLNLEQ RAWAEQLYLN ICHEVGQLFN EKHRSHRTII DELQERFADK LYVNFSLFQS 

       490        500        510        520        530        540 
LPDAWGIDQL FPVCPISNLN QPVSRRAVLL DITCDSDGTI DHYIDGDGIT TTMPMPHYEE 

       550        560        570        580        590        600 
DNPPLLGFFM VGAYQEILGN MHNLFGDTST VDVLVHEQDK AYIVDYDEGN TVADMLEYVY 

       610        620        630        640 
LDPKKLLDRY REQIEHSNLP ASEAIQFLNE LEVGLNGYTY LEDE 

« Hide

References

[1]"Complete genomic sequence of Pasteurella multocida Pm70."
May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pm70.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004439 Genomic DNA. Translation: AAK03466.1.
RefSeqNP_246321.1. NC_002663.1.

3D structure databases

ProteinModelPortalQ9CL60.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272843.PM1382.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK03466; AAK03466; PM1382.
GeneID1244729.
KEGGpmu:PM1382.
PATRIC22872023. VBIPasMul88067_1394.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPMUL272843:GC8W-1435-MONOMER.

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.
IPR022657. De-COase2_CS.
IPR022644. De-COase2_N.
IPR022653. De-COase2_pyr-phos_BS.
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.
PROSITEPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSPEA_PASMU
AccessionPrimary (citable) accession number: Q9CL60
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: June 1, 2001
Last modified: February 19, 2014
This is version 73 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