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P74576 (SPEA1_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. 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 1

Short name=ADC 1
EC=4.1.1.19
Gene names
Name:speA1
Synonyms:speA
Ordered Locus Names:slr0662
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis

Protein attributes

Sequence length695 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

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 – 695695Biosynthetic arginine decarboxylase 1 HAMAP-Rule MF_01417
PRO_0000149981

Regions

Region332 – 34211Substrate-binding Potential

Amino acid modifications

Modified residue1411N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P74576 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: E90EB699D666320D

FASTA69578,239
        10         20         30         40         50         60 
MEGQSIELEL SVMAMPELID STEAGHTAGV KTDSNPQAIA QDRRWTIDDS ENLYRITGWG 

        70         80         90        100        110        120 
EPYFSINAAG HVTVSPQADH GGALDLYELV KGLRQRNIGL PLLLRFSDIL ADRINRLNAA 

       130        140        150        160        170        180 
FARGIARYRY PNTYRGVYPI KCNQHRHIVE SLVRYGTPYN FGLEAGSKPE LMIALAMLQP 

       190        200        210        220        230        240 
QENPEPDQQN QPLLICNGYK DREYIETALL ARRLGHRPII VVEQVAEVAL AIEISSNLGI 

       250        260        270        280        290        300 
KPILGVRAKL STQGMGRWGI STGDRAKFGL TIPEMLTAIE QLRRADMLDS LQLLHFHIGS 

       310        320        330        340        350        360 
QISSISVIKE AMTEASQIFV QLAKLGANMR YLDVGGGLGV DYDGSKTNFY ASKNYNIQNY 

       370        380        390        400        410        420 
VNDVISAVQD ACVAAEVPCP VLISESGRAI ASHQSVLIFD VVATNDINPP LPKVKGKDHA 

       430        440        450        460        470        480 
ILRNLMETWE TITVDNYQEA YHDVEQFKTE AISLFNFGYL GLKERAKAEE LYWACCRKIL 

       490        500        510        520        530        540 
QICRQQEYVP DDLENLEVNL ASIYYANMSV FQSAPDSWAI DQLFPIMPIH RLDEEPTQRG 

       550        560        570        580        590        600 
ILADITCDSD GKIDQFIDLR DVKSVLELHP LIEVHQPGTP PRVEPYYLGM FLVGAYQEIM 

       610        620        630        640        650        660 
GNLHNLFGDI NVVHIQMNPK GYQIEHLVRG DTIAEVLGYV QYDPEDLLEN MRRYCEQAME 

       670        680        690 
DKRMSLEEAQ LLLENYERSL LQYTYLKPTS GIHTS 

« Hide

References

[1]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 6803 / Kazusa.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000022 Genomic DNA. Translation: BAA18683.1.
PIRS76771.
RefSeqNP_442871.1. NC_000911.1.
YP_005652932.1. NC_017277.1.
YP_007452747.1. NC_020286.1.

3D structure databases

ProteinModelPortalP74576.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP74576. 2 interactions.
STRING1148.slr0662.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA18683; BAA18683; BAA18683.
GeneID12255301.
14618437.
953209.
KEGGsyn:slr0662.
syy:SYNGTS_2979.
syz:MYO_130130.
PATRIC23843536. VBISynSp132158_3299.

Phylogenomic databases

eggNOGCOG1166.
HOGENOMHOG000029191.
KOK01585.
OMAMIHFHIG.
OrthoDBEOG676Z0R.
PhylomeDBP74576.
ProtClustDBPRK05354.

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 nameSPEA1_SYNY3
AccessionPrimary (citable) accession number: P74576
Entry history
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

SIMILARITY comments

Index of protein domains and families