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A3PA96 (SPEA_PROM0) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 54. 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:P9301_00481
OrganismProchlorococcus marinus (strain MIT 9301) [Complete proteome] [HAMAP]
Taxonomic identifier167546 [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_1000024258

Regions

Region291 – 30111Substrate-binding Potential

Amino acid modifications

Modified residue1091N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A3PA96 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 7B3791D58CCC947E

FASTA64873,366
        10         20         30         40         50         60 
MTNFEPKKLK NVWTIEDSIS TYNIDKWGDK YFSINSKGNI SVTKDIKSEN KIDLFKLVKE 

        70         80         90        100        110        120 
LKSREINPPL IIRFNDILKD RINALHDSFF KAIKTYKYKN IYQGVFPVKC NQQKNVLEKI 

       130        140        150        160        170        180 
IDFGSQWNFG LEVGSKSELL IGLALLENHN SLLICNGYKD KKYIEIATLA RKLGKNPIIV 

       190        200        210        220        230        240 
IEQRDEVKRI IQAVQELNAT PLIGIRAKLS SKSSGRWGKS IGDNSKFGLS IPEIMLTIKE 

       250        260        270        280        290        300 
LKEANLINEM KLLHFHIGSQ ISDIAVIKDA LQEASQIYVE LCKLGAPMQY IDVGGGLGID 

       310        320        330        340        350        360 
FDGTKTSSNT STNYSLQNYA NDVIATIKDS CELNNIKHPT IISESGRAII SHCSVLIFNV 

       370        380        390        400        410        420 
LGTSHVSSKL QIFDKKNQQL IISNLLETYY ELKKLKNKKI NLSQIIELWN DAKKFKEDCL 

       430        440        450        460        470        480 
VAFRLGFLSL AERAYAEELA WACAKEISNN LNNDEINHPD LSEITETLAS TYYANLSIFK 

       490        500        510        520        530        540 
SIPDSWAINQ IFPIVPIHRH LEEPFCKGNF ADLTCDSDGK LNNFIDDGKI KSLLNLHEPE 

       550        560        570        580        590        600 
KDKDYLIGIF MTGAYQEALG NLHNLFGSTN VVHIDINQDD SYKVKNIIKE DSKSEILQLL 

       610        620        630        640 
DYSSASLVES IRINTESAID QKKLTIEEAR KLMDQIEISL RKSSYLSE 

« 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 9301.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000576 Genomic DNA. Translation: ABO16671.1.
RefSeqYP_001090272.1. NC_009091.1.

3D structure databases

ProteinModelPortalA3PA96.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167546.P9301_00481.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO16671; ABO16671; P9301_00481.
GeneID4912068.
KEGGpmg:P9301_00481.
PATRIC22993689. VBIProMar103344_0049.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1166.
HOGENOMHOG000029191.
KOK01585.
OMACKGNPEA.
OrthoDBEOG676Z0R.

Enzyme and pathway databases

BioCycPMAR167546:GH1Y-50-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_PROM0
AccessionPrimary (citable) accession number: A3PA96
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 3, 2007
Last modified: June 11, 2014
This is version 54 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