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A6L012 (SPEA_BACV8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. 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:BVU_1337
OrganismBacteroides vulgatus (strain ATCC 8482 / DSM 1447 / NCTC 11154) [Complete proteome] [HAMAP]
Taxonomic identifier435590 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length630 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 – 630630Biosynthetic arginine decarboxylase HAMAP-Rule MF_01417
PRO_1000024256

Regions

Region281 – 29111Substrate-binding Potential

Amino acid modifications

Modified residue991N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A6L012 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: 9396373E70A8C266

FASTA63071,488
        10         20         30         40         50         60 
MRKWRIEDSE ELYNITGWGT SYFGINDKGH VVVTPRKDGV EVDLKELVDE LQLRDVAAPM 

        70         80         90        100        110        120 
LVRFPDILDN RIEKIANCFK QASDEYGYKA QNFIIYPIKV NQMRPVVEEI ISHGKKFNLG 

       130        140        150        160        170        180 
LEAGSKPELH AVIAVNTDSD SLIICNGYKD ESYIELALLA QKMGKRIFLV VEKMNELRLI 

       190        200        210        220        230        240 
AKMAKQLNVR PNIGIRIKLA SSGSGKWEDS GGDASKFGLT SSELLEALDF LEKKDMKDCL 

       250        260        270        280        290        300 
KLIHFHIGSQ VTKIRRIKTA LREASQFYVQ LHVMGFNVEF VDIGGGLGVD YDGTRSANSE 

       310        320        330        340        350        360 
SSVNYSIQEY VNDSISTLVD ASDKNGIPHP NIITESGRSL TAHHSVLIFE VLETATLPEM 

       370        380        390        400        410        420 
DEDFEVGEND HELVHELYEI WDNLNQSRMV EAWHDAQQIR EEALDLFSHG IVDLKTRAQI 

       430        440        450        460        470        480 
ERLYWSVTRE INQIASGLKH APDEFRKLDK LLADKYFCNF SLFQSLPDSW AIDQIFPIMP 

       490        500        510        520        530        540 
IQRLDEKPDR NATLQDITCD SDGKIANFIS TRYVSHDLPV HSLKGKDAYY IGVFLVGAYQ 

       550        560        570        580        590        600 
EILGDMHNLF GDTNAVHVTV DDKGYSIDQV IDGETVAEVL DYVQYNPKKL VRTLETWVTK 

       610        620        630 
SVKEGRISVE EGKEFLSNYR SGLYGYTYLE 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000139 Genomic DNA. Translation: ABR39026.1.
RefSeqYP_001298648.1. NC_009614.1.

3D structure databases

ProteinModelPortalA6L012.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING435590.BVU_1337.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR39026; ABR39026; BVU_1337.
GeneID5302303.
KEGGbvu:BVU_1337.
PATRIC21067514. VBIBacVul85104_1390.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBVUL435590:GH96-1334-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_BACV8
AccessionPrimary (citable) accession number: A6L012
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 24, 2007
Last modified: February 19, 2014
This is version 51 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