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A5GWM2 (SPEA_SYNR3) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 35. 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:SynRCC307_2378
OrganismSynechococcus sp. (strain RCC307) [Complete proteome] [HAMAP]
Taxonomic identifier316278 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Chroococcales › Synechococcus

Protein attributes

Sequence length640 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the biosynthesis of agmatine from arginine By similarity. HAMAP MF_01417

Catalytic activity

L-arginine = agmatine + CO2. HAMAP MF_01417

Cofactor

Magnesium By similarity. HAMAP MF_01417

Pyridoxal phosphate By similarity. HAMAP MF_01417

Pathway

Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1. HAMAP 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 – 640640Biosynthetic arginine decarboxylase HAMAP MF_01417
PRO_1000024276

Regions

Region291 – 30111Substrate-binding Potential

Amino acid modifications

Modified residue1091N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5GWM2 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: B62EFE2DF8DD1705

FASTA64069,862
        10         20         30         40         50         60 
MVVAPSQVEQ QNWTPAASAQ LYGLDQWGDP YFSVNARGHV LVQPRGDRGG SLDLVELVEG 

        70         80         90        100        110        120 
LQSRDLQLPL LIRFEDILED RLERLHGAFE RAIAQYGYGG HYQGVFPVKC NQQRHVVEQL 

       130        140        150        160        170        180 
VESGRRWHFG LEAGSKAELL IALSLLDDPK ALLICNGYKD QRYIETAILA RQLGRQPVVV 

       190        200        210        220        230        240 
IEQADEVPRI IEASRNLGAA PLIGVRAKLS TRSTGRWGSS VGEKAKFGLS IPDLLATVEA 

       250        260        270        280        290        300 
LRDADLLGDL RLLHFHVGSQ ICDIAVLKDA LQEAGQLYVQ LASLGAPMGF LDVGGGLGVD 

       310        320        330        340        350        360 
YDGSRSATAA STNYSLQNYA NDVVATIREC CEPQGIVVPT LVSESGRAIA SHFSVLVFNV 

       370        380        390        400        410        420 
LGQSGVNQPS IPEAVEGEAL IVRNLRETLS GIGPDNLQEA WNDALKFKDD ALAAFRLGYL 

       430        440        450        460        470        480 
SLTERGKAEQ LYWACCSAIA DLLPGEEELP DELKGLKAAF ASTYYANLSV FRSAPDTWAI 

       490        500        510        520        530        540 
DQLFPVMPIH RLEEQPRELG SFADLTCDSD GKLARFIASG SAKPLLELHE LKDGEPYWIG 

       550        560        570        580        590        600 
LFLGGAYQEV MGNLHNLFGS TNAVSIRLSP GGPYRVEHVV RGQTNSDVLE AMEHNPEALL 

       610        620        630        640 
ERLRQASEEA IGSGDLSISA ARRLMQHLEG SLRQTTYLEE

« Hide

References

[1]Genoscope
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RCC307.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CT978603 Genomic DNA. Translation: CAK29281.1.
RefSeqYP_001228634.1. NC_009482.1.

3D structure databases

ProteinModelPortalA5GWM2.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5GWM2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5156587.
GenomeReviewsGene locus SynRCC307_2378 in contig CT978603_GR.
KEGGsyr:SynRCC307_2378.
PATRIC23825709. VBISynSp108374_2389.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1166.
HOGENOMHBG321436.
OMALICNGYK.
PhylomeDBA5GWM2.
ProtClustDBPRK05354.

Family and domain databases

HAMAPMF_01417. SpeA.
[Tree]
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]
Gene3DG3DSA:2.40.37.10. Ala_racemase/Decarboxylase_C. 2 hits.
KOK01585.
PANTHERPTHR11482:SF3. Arg_decrbxlase. 1 hit.
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. Racem_decarbox_C. 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_SYNR3
AccessionPrimary (citable) accession number: A5GWM2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 12, 2007
Last modified: December 14, 2011
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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