Skip Header

Contribute Send feedback
Read comments (?) or add your own

B0JUQ5 (B0JUQ5_MICAN) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

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:MAE_46810
OrganismMicrocystis aeruginosa (strain NIES-843) [Complete proteome] [HAMAP]
Taxonomic identifier449447 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Chroococcales › Microcystis

Protein attributes

Sequence length679 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. RuleBase RU003740 HAMAP MF_01417 SAAS SAAS009006

Cofactor

Magnesium By similarity. RuleBase RU003740 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

Region322 – 33211Substrate-binding By similarity HAMAP MF_01417

Amino acid modifications

Modified residue1321N6-(pyridoxal phosphate)lysine By similarity HAMAP MF_01417

Sequences

Sequence LengthMass (Da)Tools
B0JUQ5 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: 1D50F54F9A22A824

FASTA67976,705
        10         20         30         40         50         60 
MAGKTQLKKQ EKQLSQLDLT PSDGNNLEKV APVKHWSIED SENLYRIQGW GEPYFSINAA 

        70         80         90        100        110        120 
GNITVSPQGE RGGSLDLYEL VSAIKRRNIG LPLLIRFSDI LEDRIERLNA CFSRAIARYN 

       130        140        150        160        170        180 
YPNVYRGVYP IKCNQHRHIV ESLVRFGKPY QFGLEAGSKP ELMIALATLE PALNGKNDKT 

       190        200        210        220        230        240 
QPLLICNGYK DKEYIETALL TTRLGHRPLI VIEQLEELYL TLRVSRQLGI APHLGVRAKL 

       250        260        270        280        290        300 
GTKGVGRWGC STGDRAKFGL TVPEILTVVT ELEQAGMLDC LQLLHYHIGS QISAISVIKD 

       310        320        330        340        350        360 
AIREASQIYV ELAKLGANMT YLDVGGGLGV DYDGSKTNFY ASKNYNMQNY ANDIVAEVKE 

       370        380        390        400        410        420 
ACEDAQISPP ILISESGRAI ASHQSVLVFD ILGSSEVPQN PPDPCNGKEH LILRNLWETY 

       430        440        450        460        470        480 
TGIDERNYQE AYHDAGQFKE EAISLFNFGY LSLKERARAE QLYWACCHKI LQVARQEDYV 

       490        500        510        520        530        540 
PDDLEDLEQI MASIYYANLS VFQSVPDSWA IDQLFPIMPI HRLDREPTQR GILADLTCDS 

       550        560        570        580        590        600 
DGKIAQFIDL RGDIKSVLEL HPLEYKNGKH SPEPYYLGMF LVGAYQEIMG NLHNLFGDTN 

       610        620        630        640        650        660 
VVHIQMSPKG YDIEYLVKGD TITEVLSYVQ YSAEDLLERI RLRCEQALQE NRMTVEESQL 

       670 
LLQDYERSLR RYTYLVGGD

« Hide

References

[1]"Complete genomic structure of the bloom-forming toxic cyanobacterium Microcystis aeruginosa NIES-843."
Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M., Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A., Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M. expand/collapse author list , Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.
DNA Res. 14:247-256(2007) [PubMed: 18192279] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP009552 Genomic DNA. Translation: BAG04503.1.
RefSeqYP_001659695.1. NC_010296.1.

3D structure databases

ProteinModelPortalB0JUQ5.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0JUQ5.

Proteomic databases

PRIDEB0JUQ5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5865512.
GenomeReviewsGene locus MAE_46810 in contig AP009552_GR.
KEGGmar:MAE_46810.
PATRIC22633911. VBIMicAer59304_4265.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG321436.
OMALICNGYK.
PhylomeDBB0JUQ5.
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.
TIGRFAMsTIGR01273. SpeA. 1 hit.
PROSITEPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB0JUQ5_MICAN
AccessionPrimary (citable) accession number: B0JUQ5
Entry history
Integrated into UniProtKB/TrEMBL: March 18, 2008
Last sequence update: March 18, 2008
Last modified: December 14, 2011
This is version 25 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