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Q3AGN9 (Q3AGN9_SYNSC) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 43. 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 MF_01417
Short name=ADC HAMAP MF_01417
EC=4.1.1.19 HAMAP MF_01417
Gene names
Name:speA HAMAP MF_01417
Ordered Locus Names:Syncc9605_2513
OrganismSynechococcus sp. (strain CC9605) [Complete proteome] [HAMAP]
Taxonomic identifier110662 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Chroococcales › Synechococcus

Protein attributes

Sequence length642 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the biosynthesis of agmatine from arginine By similarity. HAMAP MF_01417 SAAS SAAS009006

Catalytic activity

L-arginine = agmatine + CO2. HAMAP MF_01417 RuleBase RU003740 SAAS SAAS009006

Cofactor

Magnesium By similarity. HAMAP MF_01417 RuleBase RU003740 SAAS SAAS009006

Pyridoxal phosphate By similarity. HAMAP MF_01417 SAAS SAAS000183

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. HAMAP MF_01417

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region285 – 29511Substrate-binding By similarity HAMAP MF_01417

Amino acid modifications

Modified residue1031N6-(pyridoxal phosphate)lysine By similarity HAMAP MF_01417

Sequences

Sequence LengthMass (Da)Tools
Q3AGN9 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 75C1AA41B5640879

FASTA64270,609
        10         20         30         40         50         60 
MSDSEHWSIQ DSAALYGLDR WGDPYFSING RGHISVQPQG DRGGSLDLVD LVSELKSRNL 

        70         80         90        100        110        120 
ALPLLIRFDD ILEDRLERLH AAFERAIAQY SYAGRYQGVF PVKCNQQRHV VEELVSCGKR 

       130        140        150        160        170        180 
WNFGLEAGSK AELLIALSLL DDPEALLICN GYKDRLYIET AILARRLGRQ PVVVIEQPDE 

       190        200        210        220        230        240 
VDRIIEASKS LGAAPYIGVR AKLSSRSTGR WGSSVGDKAK FGLSIPELLA TVERLRDNNL 

       250        260        270        280        290        300 
LQDLRLLHFH IGSQINDIAV LKDALQEAGQ IYVELTRLGA PMGFLDVGGG LGIDYDGSRT 

       310        320        330        340        350        360 
ASAASTNYSL QNYANDVVAT VRECCEPNGV AVPTLVSESG RAIASHFSLL VFDVLGSSSL 

       370        380        390        400        410        420 
PASVPKASGD EPLTVRNLRD TLATIQELSA TTDAQLVRLQ EAWNDALKFK QDALAAFRLG 

       430        440        450        460        470        480 
YMSLPDRATA EQLTWACADG IAQRLPQDQA IPEELAALNK ALAGTYYANL SIFRSAPDTW 

       490        500        510        520        530        540 
AIDQLFPVVP IQQLDQRPTR LANLADLTCD SDGRLDRFIG DGQPKQLLEL HELDGDNLYL 

       550        560        570        580        590        600 
IGLFLSGAYQ EVMGNLHNLF GTTNAVHIRL SPGGSYRIDH VVRGDTNADV LEAMEHDPRT 

       610        620        630        640 
LLERLRVAAE AAINNGQLRI DESRRLLDHL ESSLRQTTYL QD

« Hide

References

[1]"Complete sequence of Synechococcus sp. CC9605."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CC9605.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000110 Genomic DNA. Translation: ABB36243.1.
RefSeqYP_382798.1. NC_007516.1.

3D structure databases

ProteinModelPortalQ3AGN9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3AGN9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3737928.
GenomeReviewsGene locus Syncc9605_2513 in contig CP000110_GR.
KEGGsyd:Syncc9605_2513.
NMPDRfig|110662.3.peg.1140.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1166.
HOGENOMHBG321436.
OMALICNGYK.
PhylomeDBQ3AGN9.
ProtClustDBPRK05354.

Enzyme and pathway databases

BioCycSSP1131:SYNCC9605_2513-MONOMER.

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.
TIGRFAMsTIGR01273. SpeA. 1 hit.
PROSITEPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ3AGN9_SYNSC
AccessionPrimary (citable) accession number: Q3AGN9
Entry history
Integrated into UniProtKB/TrEMBL: November 22, 2005
Last sequence update: November 22, 2005
Last modified: December 14, 2011
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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