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Q2JXW4 (Q2JXW4_SYNJA) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Biosynthetic arginine decarboxylase HAMAP-Rule MF_01417
Short name=ADC HAMAP-Rule MF_01417
EC=4.1.1.19 HAMAP-Rule MF_01417
Gene names
Name:speA HAMAP-Rule MF_01417
Ordered Locus Names:CYA_0128
OrganismSynechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone A-Prime) [Complete proteome] [HAMAP] EMBL ABC98358.1
Taxonomic identifier321327 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechococcus

Protein attributes

Sequence length641 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 SAAS SAAS022644 RuleBase RU003740

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01417 RuleBase RU003740 SAAS SAAS022644

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01417 SAAS SAAS022644

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. HAMAP-Rule MF_01417

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region289 – 29911Substrate-binding By similarity HAMAP-Rule MF_01417

Amino acid modifications

Modified residue1071N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01417

Sequences

Sequence LengthMass (Da)Tools
Q2JXW4 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: EBB985E2495BED69

FASTA64171,853
        10         20         30         40         50         60 
MPTLTRSPWT LRDSEKLYRI SGWGDPYFRI NAAGHVEVTP QGSQQQEGGI DLYHLVTDLV 

        70         80         90        100        110        120 
ARGLQLPLLI RFPEIVADRM RRICESFQQA IERFGYPNVY RGVYPVKVNQ QRHLVEEVVK 

       130        140        150        160        170        180 
HGRAYHFGLE AGSKPELLIA LALLDTPGAL LICNGYKDRD FMETALLAQR LGRTPIIVLE 

       190        200        210        220        230        240 
RLQELELVLQ AAEHLGIDPL LGVRAKLSAQ GSGRWGTSAG DRGKFGLTAT EMLQVVERLR 

       250        260        270        280        290        300 
EVGKLHCLRL LHYHIGSQIS MVSVHGRAVR EASQIYIELV KLGAPMGYLD VGGGLGVDYD 

       310        320        330        340        350        360 
GSQSTSHFSQ SYSLEDYAAT VVQTVLTALQ PHGIQPPVLV TESGRALMSH QSVLVFDIQD 

       370        380        390        400        410        420 
VNAASPYPMP TQLTSDAEVI QKLNQLYYEI RPETLVADYR RCQELKEAAL RQFTEGSLSL 

       430        440        450        460        470        480 
RERAEVERLF WNCSDKICTL AYEQHQAGQP VAVDLLDLDE MLASIYYGNF SLFQSLPDSW 

       490        500        510        520        530        540 
AIDQVFPIMP IHRLDEEPRQ WATLADLTCD SDGKINRFFG EDGQITSVLP LHDPNGQPYL 

       550        560        570        580        590        600 
LGVFLGGAYQ EILGDLHNLF GDTNAVHIRT RPGGYQVTQV IKGDTIGEVL SWVQYNSEDL 

       610        620        630        640 
VETLHHATEA ALQRGQITLE QARALQQHFE DNLRAYTYLH R

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References

[1]"Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses."
Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.
ISME J. 1:703-713(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JA-3-3Ab.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000239 Genomic DNA. Translation: ABC98358.1.
RefSeqYP_473621.1. NC_007775.1.

3D structure databases

ProteinModelPortalQ2JXW4.
ModBaseSearch...

Protein-protein interaction databases

STRING321327.CYA_0128.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC98358; ABC98358; CYA_0128.
GeneID3898650.
KEGGcya:CYA_0128.
PATRIC23808517. VBISynSp90045_0127.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1166.
HOGENOMHOG000029191.
KOK01585.
OMAMIHFHIG.
ProtClustDBPRK05354.

Enzyme and pathway databases

UniPathwayUPA00186; UER00284.

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]
PANTHERPTHR11482:SF3. PTHR11482:SF3. 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.
TIGRFAMsTIGR01273. speA. 1 hit.
PROSITEPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ2JXW4_SYNJA
AccessionPrimary (citable) accession number: Q2JXW4
Entry history
Integrated into UniProtKB/TrEMBL: March 7, 2006
Last sequence update: March 7, 2006
Last modified: May 1, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info