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A8G243 (SPEA_PROM2) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 51. 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:P9215_00551
OrganismProchlorococcus marinus (strain MIT 9215) [Complete proteome] [HAMAP]
Taxonomic identifier93060 [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_1000068493

Regions

Region291 – 30111Substrate-binding Potential

Amino acid modifications

Modified residue1091N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A8G243 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 3472447352E0C4E6

FASTA64873,405
        10         20         30         40         50         60 
MTNFEPKKLK KNWTIEDSIS TYEIDKWGDK YFSINSKGNI SVTKDINSEK KIDLFKLVRE 

        70         80         90        100        110        120 
LKSREINTPL IIRFNDILKD RINALHDAFL KAIKTYKYKN IYQGVFPVKC NQQKNVLEKI 

       130        140        150        160        170        180 
IEFGSPWNFG LEVGSKSELL IGLALLENQN SLLICNGYKD KKYIEIATLA RKLGKNPIIV 

       190        200        210        220        230        240 
IEQKDEVNRI IEAVQDLNAS PLIGIRAKLS SKSSGRWSKS VGDNSKFGLS IPEIMSTIKE 

       250        260        270        280        290        300 
LKEANLINEM RLLHFHIGSQ ISDIAVIKDA LQEASQIYVE LFKLGAPMKY IDVGGGLGID 

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

       370        380        390        400        410        420 
LGTSHVSSKL KIYDDKKQSL IISNLIETFY ELKKLKNKKI NLSQIIELWN DAKKFKEDCL 

       430        440        450        460        470        480 
VAFRLGFLSL AERAYAEELT WACAKEIANN LNNDEINHPD LFEITETLAS TYYANLSIFK 

       490        500        510        520        530        540 
SIPDCWAINQ IFPIMPIHRH LEEPFCKGNF ADLTCDSDGK LNSFINNGKI KSLLNLHEPE 

       550        560        570        580        590        600 
QDKDYLIGIF MTGAYQEALG NLHNLFGNTN VVHIDINQND SYKVKNIIKE DSKSEILQLL 

       610        620        630        640 
DYSSASLVES IRINTEAAID QKKLTIEEAR KLIDQIEISL 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 9215.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000825 Genomic DNA. Translation: ABV49674.1.
RefSeqYP_001483260.1. NC_009840.1.

3D structure databases

ProteinModelPortalA8G243.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93060.P9215_00551.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV49674; ABV49674; P9215_00551.
GeneID5615874.
KEGGpmh:P9215_00551.
PATRIC22989523. VBIProMar119824_0056.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1166.
HOGENOMHOG000029191.
KOK01585.
OMAANIRDIH.
OrthoDBEOG676Z0R.

Enzyme and pathway databases

BioCycPMAR93060:GI08-57-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_PROM2
AccessionPrimary (citable) accession number: A8G243
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 13, 2007
Last modified: June 11, 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