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Q7N121 (SPEA_PHOLL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 70. 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:plu3681
OrganismPhotorhabdus luminescens subsp. laumondii (strain TT01) [Complete proteome] [HAMAP]
Taxonomic identifier243265 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePhotorhabdus

Protein attributes

Sequence length634 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 – 634634Biosynthetic arginine decarboxylase HAMAP-Rule MF_01417
PRO_0000149967

Regions

Region283 – 29311Substrate-binding Potential

Amino acid modifications

Modified residue1031N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7N121 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: A3268D93070FDCB5

FASTA63471,155
        10         20         30         40         50         60 
MNDNIARKMQ QTYNIAYWGG SYYYVNDLGN VSVCPNPDLP GAKIDLAELV KRVQQEQKHL 

        70         80         90        100        110        120 
RLPALFCFPQ ILQHRLRSIN AAFKRARESY GYKGDYFLVY PIKVNQQRRV IESLASSGEP 

       130        140        150        160        170        180 
LGLEAGSKAE LMAVLAHAGM TRTVIVCNGY KDREYIRLAL IGEKLGHKVY LVIEKMSEIA 

       190        200        210        220        230        240 
QVLEEAERLN VIPRLGVRAR LASQGSGKWQ ASGGEKSKFG LAATQVLQLV ETLRAVDRLD 

       250        260        270        280        290        300 
SLQLLHFHLG SQLANIRDIA TGVRESARFY VELHKLGVNI QCFDVGGGLG VDYEGTRSQS 

       310        320        330        340        350        360 
DCSVNYGLNE YANNVIWGIG DACDEHGLPH PTVITESGRA LTAHHTVLVS NVIGVERNEF 

       370        380        390        400        410        420 
TQTTPPAEDA SRPLTSLWET WQEMHSEGNR RSLRESLHDG QLDLHDVHTQ YAHGMLDLTE 

       430        440        450        460        470        480 
RAWAEELYLN ICRRIQQDLD PSNRAHRPII DELQERMADK FYVNFSLFQS LPDAWGIDQL 

       490        500        510        520        530        540 
FPVLPIEGLD KPLDRRAVLL DITCDSDGIV DHYVDGDGVA ATMPMPAYDP DCPPMIGFFM 

       550        560        570        580        590        600 
VGAYQEILGN MHNLFGDTAA IDVYVFDNGE VTYNQSEEGD SVADMLQYVK LDPNVLMARF 

       610        620        630 
RDQVKGADLD TGLQEQFLLE FESGLYGYTY LEDE 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX571871 Genomic DNA. Translation: CAE16054.1.
RefSeqNP_930889.1. NC_005126.1.

3D structure databases

ProteinModelPortalQ7N121.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243265.plu3681.

Proteomic databases

PRIDEQ7N121.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE16054; CAE16054; plu3681.
GeneID2803693.
KEGGplu:plu3681.
PATRIC20511872. VBIPhoLum48522_4177.

Organism-specific databases

GenoListplu3681.
CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

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_PHOLL
AccessionPrimary (citable) accession number: Q7N121
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: December 15, 2003
Last modified: February 19, 2014
This is version 70 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