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B4F1A4 (SPEA_PROMH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 40. 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:PMI2094
OrganismProteus mirabilis (strain HI4320) [Complete proteome] [HAMAP]
Taxonomic identifier529507 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

Protein attributes

Sequence length635 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 – 635635Biosynthetic arginine decarboxylase HAMAP-Rule MF_01417
PRO_1000145597

Regions

Region283 – 29311Substrate-binding Potential

Amino acid modifications

Modified residue1031N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B4F1A4 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 3EA47042A44DCA3C

FASTA63571,775
        10         20         30         40         50         60 
MNDNIARKMQ QTYNITYWGG GYYCANNRGN ISVCPNPDVP EATLDLTELV KQVQEEHSHL 

        70         80         90        100        110        120 
RLPALFCFPQ ILQHRLRSIN AAFHRARESY GYKGDYFLVY PIKVNQQRRV IESLINAGEP 

       130        140        150        160        170        180 
LGLEAGSKAE LMAVLAHANM TSSVIVCNGY KDREYIRLAL TGEKLGHKVF LVIEKMSEIK 

       190        200        210        220        230        240 
MVLEEAERLE VIPRLGVRAR LASQGSGKWQ ASGGEKSKFG LAATQVLQLI DTLRQAGRLD 

       250        260        270        280        290        300 
SLQLLHFHLG SQMANIRDIA TGVRESARFY VELHKLGVNI QYFDVGGGLG VDYEGTRSQS 

       310        320        330        340        350        360 
DCSVNYGLNE YANNVIWAIG DACDENELPH PTVITESGRA LTAHHTVLIS NVIGVERNEF 

       370        380        390        400        410        420 
TAITPPAEDA PRPIASLWET WEEMQTKGNS RSLREWLHDS QLDLHDVHTQ YVHGMLSLTE 

       430        440        450        460        470        480 
RAWAEELYLN ICRHIQYDLD PSNRAHRPII DELQERMSDK FYVNFSLFQS LPDAWGIDQL 

       490        500        510        520        530        540 
FPVLPIEGLD KPLDRRAVLL DITCDSDGII DHYVDGDGVE TTMPMPAYDP EYPPMIGFFM 

       550        560        570        580        590        600 
VGAYQEILGN MHNLFGDTAA VDVYLDEKGN LTYQLSEEGD TVADMLQYVK LNPAVLLERF 

       610        620        630 
RTQVKNAQLD KALQEQFLTE FESGLYGYTY LEEEE 

« Hide

References

[1]"Complete genome sequence of uropathogenic Proteus mirabilis, a master of both adherence and motility."
Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S., Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T., Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Walker D., Whithead S. expand/collapse author list , Thomson N.R., Rather P.N., Parkhill J., Mobley H.L.T.
J. Bacteriol. 190:4027-4037(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HI4320.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM942759 Genomic DNA. Translation: CAR44185.1.
RefSeqYP_002151813.1. NC_010554.1.

3D structure databases

ProteinModelPortalB4F1A4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING529507.PMI2094.

Proteomic databases

PRIDEB4F1A4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR44185; CAR44185; PMI2094.
GeneID6803159.
KEGGpmr:PMI2094.
PATRIC20518867. VBIProMir120933_2043.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPMIR529507:GJIW-2130-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.
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_PROMH
AccessionPrimary (citable) accession number: B4F1A4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: February 19, 2014
This is version 40 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