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Q8A2B1 (SPEA_BACTN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 74. 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:BT_3394
OrganismBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482) [Reference proteome] [HAMAP]
Taxonomic identifier226186 [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

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_0000149957

Regions

Region281 – 29111Substrate-binding Potential

Amino acid modifications

Modified residue991N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8A2B1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: C124255A68131F19

FASTA63071,246
        10         20         30         40         50         60 
MRKWRIEDSE ELYNITGWGT SYFSINDAGH VVVTPRRDGV TVDLKELVDE LQLRDVASPM 

        70         80         90        100        110        120 
LLRFPDILDN RIEKMSSCFK QAAEEYGYKA ENFIIYPIKV NQMRPVVEEI ISHGKKFNLG 

       130        140        150        160        170        180 
LEAGSKPELH AVIAVNTDSD SLIVCNGYKD ESYIELALLA QKMGKRIFLV VEKMNELKLI 

       190        200        210        220        230        240 
AKMAKQLNVQ PNIGIRIKLA SSGSGKWEES GGDASKFGLT SSELLEALDF MESKGLKDCL 

       250        260        270        280        290        300 
KLIHFHIGSQ VTKIRRIKTA LREASQFYVQ LHSMGFNVEF VDIGGGLGVD YDGTRSSNSE 

       310        320        330        340        350        360 
GSVNYSIQEY VNDSISTLVD VSDKNGIPHP NIITESGRAL TAHHSVLIFE VLETATLPEW 

       370        380        390        400        410        420 
DDEEEIAPDA HELVQELYSI WDSLNQNKML EAWHDAQQIR EEALDLFSHG IVDLKTRAQI 

       430        440        450        460        470        480 
ERLYWSITRE INQIAGGLKH APDEFRGLSK LLADKYFCNF SLFQSLPDSW AIDQIFPIMP 

       490        500        510        520        530        540 
IQRLDEKPER SATLQDITCD SDGKIANFIS TRNVAHYLPV HSLKKTEPYY LAVFLVGAYQ 

       550        560        570        580        590        600 
EILGDMHNLF GDTNAVHVSV NEKGYNIEQI IDGETVAEVL DYVQYNPKKL VRTLETWVTK 

       610        620        630 
SVKEGKISLE EGKEFLSNYR SGLYGYTYLE 

« Hide

References

[1]"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
Science 299:2074-2076(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015928 Genomic DNA. Translation: AAO78500.1.
RefSeqNP_812306.1. NC_004663.1.

3D structure databases

ProteinModelPortalQ8A2B1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING226186.BT_3394.

Protocols and materials databases

DNASU1075986.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO78500; AAO78500; BT_3394.
GeneID1075986.
KEGGbth:BT_3394.
PATRIC21061801. VBIBacThe70966_3462.

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBTHE226186:GJXV-3459-MONOMER.

Family and domain databases

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_BACTN
AccessionPrimary (citable) accession number: Q8A2B1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 74 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