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Q3AVV4 (Q3AVV4_SYNS9) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 40. 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:Syncc9902_2172
OrganismSynechococcus sp. (strain CC9902) [Complete proteome] [HAMAP] EMBL ABB27130.1
Taxonomic identifier316279 [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 SAAS SAAS009006

Cofactor

Magnesium By similarity. HAMAP MF_01417 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
Q3AVV4 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 18BE87B60A09486B

FASTA64270,714
        10         20         30         40         50         60 
MADGEGWSIQ NSTELYGLER WGDPYFSINA RGHISVQPQG ERGGSLDLHE LVQELRSRNL 

        70         80         90        100        110        120 
SLPLLIRFDD ILEDRLERLH SAFERAIAQY GYKGRYQGVF PVKCNQQRHV VEELVSCGKR 

       130        140        150        160        170        180 
WNFGLEAGSK AELLIALSLL DDPDALLICN GYKDRLYIET AILARRLGRR PVVVIEQPDE 

       190        200        210        220        230        240 
VDRIIEASRN LGAAPYIGIR AKLASRSTGR WGSSVGDKAK FGLAIPDLLT TVERLRDNGL 

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

       310        320        330        340        350        360 
ATAASTNYSL QNYANDVVAT VRECCEPNGV ALPTLVSESG RAIASHFSLL VFDVLGSSRM 

       370        380        390        400        410        420 
PASIPPATED EPLIVRNLRS TLETIHNLDG SDQADLPPLQ EAWNDALKFK QDALAAFRLG 

       430        440        450        460        470        480 
YAGLPERATA EQLTWACAAA IAERLPTGPS VPEELQALKA ALAETYYANL SVFRSAPDTW 

       490        500        510        520        530        540 
AIDQIFPVVP LQRLEERPTL LASLADLTCD SDGRLNRFIG NGQAKPLLEL HPLINDEPYF 

       550        560        570        580        590        600 
IGLFLSGAYQ EVMGNLHNLF GTTNAVHIRL SPGGSYRVDH VVRGDTNADV LKAMEHDPDL 

       610        620        630        640 
LLERLRVAAE GAISNGQLRI EESRRLLDHL ESSLRQTTYL QD

« Hide

References

[1]"Complete sequence of Synechococcus sp. CC9902."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000097 Genomic DNA. Translation: ABB27130.1.
RefSeqYP_378173.1. NC_007513.1.

3D structure databases

ProteinModelPortalQ3AVV4.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3AVV4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3742664.
GenomeReviewsGene locus Syncc9902_2172 in contig CP000097_GR.
KEGGsye:Syncc9902_2172.
PATRIC23801923. VBISynSp76179_2392.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1166.
HOGENOMHBG321436.
OMALICNGYK.
PhylomeDBQ3AVV4.
ProtClustDBPRK05354.

Enzyme and pathway databases

BioCycSSP1131-1:SYNCC9902_2172-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 nameQ3AVV4_SYNS9
AccessionPrimary (citable) accession number: Q3AVV4
Entry history
Integrated into UniProtKB/TrEMBL: November 22, 2005
Last sequence update: November 22, 2005
Last modified: December 14, 2011
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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