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A2CDK1 (SPEA_PROM3) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 55. 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:P9303_28311
OrganismProchlorococcus marinus (strain MIT 9303) [Complete proteome] [HAMAP]
Taxonomic identifier59922 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length648 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 – 648648Biosynthetic arginine decarboxylase HAMAP-Rule MF_01417
PRO_1000024259

Regions

Region291 – 30111Substrate-binding Potential

Amino acid modifications

Modified residue1091N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A2CDK1 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: 648B16E4961C51D0

FASTA64871,351
        10         20         30         40         50         60 
MSAADPSQGN KSWTVADSAA LYGLDRWGEP YFTANANGHV QVKPRGDQGS CLDLVELVEE 

        70         80         90        100        110        120 
LKSRNLNLPL LIRFDDILED RLEKLHSAFE QAISKYGYAG RYQGVFPVKC NQQRHVVEQL 

       130        140        150        160        170        180 
VESGRHWHFG LEAGSKAELL IALSLVNDPE ALLICNGYKD QRYIETAILA RRLGRQPVVV 

       190        200        210        220        230        240 
IEQPDEVERI IRSSQELGAA PFIGVRAKLT TRSTGHWSSS VGEKAKFGLS FPDLLSTVEA 

       250        260        270        280        290        300 
LRQADLLSDL RLLHFHIGSQ INDIAVLKDA IQEAGQIYVE LTKLGAPMGY LDVGGGLGVD 

       310        320        330        340        350        360 
YDGSRSASAA STNYSLQNYA NDVVATVREC CKPHGITLPI LVSESGRAIA SHFSILVFDV 

       370        380        390        400        410        420 
LGTGTVPGAV PNQTGEEPLT IHNLRETLAG VMATQKGAAS EISRLQEAWN DAVKFKDDAL 

       430        440        450        460        470        480 
AAFRLGYISL TERALAEQLT WACAEAIMGQ LPCHETIPDD LQGLRAVLAG TYYANLSIFR 

       490        500        510        520        530        540 
SAPDTWAIEQ LFPLMPIHRL KEEPTQLGHF ADLTCDSDGK LDRFIGNGQT KTLLELHNLR 

       550        560        570        580        590        600 
QNEAYMIGMF LAGAYQEVMG NLHNLFGSTN AVHIRMTTGG GYQIDHVVRG NTNSEVLEAM 

       610        620        630        640 
EHNPEILLER LRLASELAIQ RGELKINDVR RLMDHLETSL RQTTYLQG 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9303.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000554 Genomic DNA. Translation: ABM79561.1.
RefSeqYP_001018826.1. NC_008820.1.

3D structure databases

ProteinModelPortalA2CDK1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59922.P9303_28311.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM79561; ABM79561; P9303_28311.
GeneID4776972.
KEGGpmf:P9303_28311.
PATRIC23003209. VBIProMar17757_2888.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1166.
HOGENOMHOG000029191.
KOK01585.
OMAIDHYVDG.
OrthoDBEOG676Z0R.

Enzyme and pathway databases

BioCycPMAR59922:GH54-2941-MONOMER.
UniPathwayUPA00186; UER00284.

Family and domain databases

Gene3D2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
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.
IPR029066. PLP-binding_barrel.
[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.
SSF51419. SSF51419. 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_PROM3
AccessionPrimary (citable) accession number: A2CDK1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 20, 2007
Last modified: June 11, 2014
This is version 55 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