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A2BU00 (SPEA_PROM5) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Biosynthetic arginine decarboxylase

Short name=ADC
EC=4.1.1.19
Gene names
Name:speA
Ordered Locus Names:P9515_00521
OrganismProchlorococcus marinus (strain MIT 9515) [Complete proteome] [HAMAP]
Taxonomic identifier167542 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length648 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

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 648648Biosynthetic arginine decarboxylase HAMAP-Rule MF_01417
PRO_1000024260

Regions

Region291 – 30111Substrate-binding Potential

Amino acid modifications

Modified residue1091N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A2BU00 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: FAD4EF01EC8D33A4

FASTA64873,324
        10         20         30         40         50         60 
MTNFDSKKLN KHWTIEDSIS TYGIDKWGDQ YFSINSLGNI SITPNRNSKK TIDLFKLVNE 

        70         80         90        100        110        120 
IKSREINTPL ILRFNDILKD RITELNNAFS QAIETYNYKN IFQGVFPIKC NQQKNVLEKI 

       130        140        150        160        170        180 
IEYGDYWDFG LEVGSKSELL IGLSLLENKK SLLICNGYKD KKYIEIAILA RKLGKQPIIV 

       190        200        210        220        230        240 
IEQIDEVQRI IEAVKNLRST PILGIRSKLS SKSSGRWGKS VGDNSKFGLS IPEIMLTIKE 

       250        260        270        280        290        300 
LKEASLINEM KLLHFHIGSQ ISDISVIKDA LQEASQIFVE LSKLGAPMKY IDVGGGLGID 

       310        320        330        340        350        360 
FDGTKTSSNT STNYSLQNYA NDVVATIKDS CEVNNIQHPI IISESGRAIV SHCSVLIFDV 

       370        380        390        400        410        420 
LGTSHVSSQI KVSHQKKTSL IIKNLIDTHN QLKNLRNKKE DLSEIIELWN DAKKFKKDCL 

       430        440        450        460        470        480 
VAFRLGFISL GERAYAEELT WACAKEISSH LDNEKIIHPD LSEITETLSS TYYANLSVFK 

       490        500        510        520        530        540 
SIPDTWAINQ IFPIIPIHRH LEEPICKGNF ADLTCDSDGK LNNFIDNGKI KSLLNLHRPE 

       550        560        570        580        590        600 
ENNDYLIGIF MAGAYQEALG NFHNLFGNTN VIHIDINEDN TYKIKNIIKE NSKSEILELL 

       610        620        630        640 
DYSSDNLVES IRINTEFAIN NKTLSIEEAR KLIDQIETSL RKSSYLSE 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9515.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000552 Genomic DNA. Translation: ABM71261.1.
RefSeqYP_001010368.1. NC_008817.1.

3D structure databases

ProteinModelPortalA2BU00.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167542.P9515_00521.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM71261; ABM71261; P9515_00521.
GeneID4719928.
KEGGpmc:P9515_00521.
PATRIC23013618. VBIProMar113831_0054.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1166.
HOGENOMHOG000029191.
KOK01585.
OMAIDHYVDG.
OrthoDBEOG676Z0R.

Enzyme and pathway databases

BioCycPMAR167542:GI3N-53-MONOMER.
UniPathwayUPA00186; UER00284.

Family and domain databases

Gene3D2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
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.
IPR029066. PLP-binding_barrel.
[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.
SSF51419. SSF51419. 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 nameSPEA_PROM5
AccessionPrimary (citable) accession number: A2BU00
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 20, 2007
Last modified: June 11, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways