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A2BZG3 (A2BZG3_PROM1) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 33. 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:NATL1_00591
OrganismProchlorococcus marinus (strain NATL1A) [Complete proteome] [HAMAP] EMBL ABM74623.1
Taxonomic identifier167555 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

Protein attributes

Sequence length647 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

Region290 – 30011Substrate-binding By similarity HAMAP MF_01417

Amino acid modifications

Modified residue1081N6-(pyridoxal phosphate)lysine By similarity HAMAP MF_01417

Sequences

Sequence LengthMass (Da)Tools
A2BZG3 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: 77DE24CCB232BEEF

FASTA64772,506
        10         20         30         40         50         60 
MAVKNTNQSL SWTIQNSSEL YGIDRWGKGY FTINEKGNIS ICPNGSKNKS HDLIELLDEL 

        70         80         90        100        110        120 
ESRKLKFPLL IRFDDILEDC LKNLHKAFEK AINDYQYEGK YQGVFPIKCN QQRHVVEELI 

       130        140        150        160        170        180 
TCGSKWNFGL EAGSKPELLI GLSILENPKA LLICNGYKDQ RYIETAILAR QLGRQPIVVI 

       190        200        210        220        230        240 
EQANDVELII KSSDLLGASP LIGIRAKLSS QSSGRWSSSI GDKSKFGLSI PEILKTIKRL 

       250        260        270        280        290        300 
KEANLLNELK LLHFHLGSQI NDIGVLKDAL QEAGQIYAEL INLGAPMGYL DVGGGLGIDY 

       310        320        330        340        350        360 
DGSQTASIAS TNYSLQNYAN DVVATIKECC ESKKIPLPTL ITESGRAIAS HFSILIFNIL 

       370        380        390        400        410        420 
GKNSLPSDIP KESEKECLSV RNLRDTLVHI NSLELKQEED LAKLQEAWND SLKFKADALA 

       430        440        450        460        470        480 
AFRLGYIDLV ERAKAEQLTW ACAKTIVNQL PKNILLPKEL KKLSESLAVT YYANLSVFRS 

       490        500        510        520        530        540 
APDTWAIDQV FPIMPIHRLR KEPKKLGHFA DLTCDSDGKL DQFIDNGKIK NLLPLHEFNQ 

       550        560        570        580        590        600 
DEKYLIGLFL GGAYQEVMGN LHNLFGSTNA VHIRFTENGN YKVEHVIRGN TKSNVLEYLE 

       610        620        630        640 
HDPEILLERL RKSSELAIQG GHLKIHDAQK LIEHVEASLR QSTYLQS

« 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: 18159947] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000553 Genomic DNA. Translation: ABM74623.1.
RefSeqYP_001013888.1. NC_008819.1.

3D structure databases

ProteinModelPortalA2BZG3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA2BZG3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4780988.
GenomeReviewsGene locus NATL1_00591 in contig CP000553_GR.
KEGGpme:NATL1_00591.
PATRIC23017627. VBIProMar31285_0061.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1166.
HOGENOMHBG321436.
OMALICNGYK.
PhylomeDBA2BZG3.
ProtClustDBPRK05354.

Enzyme and pathway databases

BioCycPMAR167555:NATL1_00591-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 nameA2BZG3_PROM1
AccessionPrimary (citable) accession number: A2BZG3
Entry history
Integrated into UniProtKB/TrEMBL: February 20, 2007
Last sequence update: February 20, 2007
Last modified: December 14, 2011
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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