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A9B9E6 (A9B9E6_PROM4) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 24. 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:P9211_00521
OrganismProchlorococcus marinus (strain MIT 9211) [Complete proteome] [HAMAP] EMBL ABX07983.1
Taxonomic identifier93059 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

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 MF_01417

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

Region291 – 30111Substrate-binding By similarity HAMAP MF_01417

Amino acid modifications

Modified residue1091N6-(pyridoxal phosphate)lysine By similarity HAMAP MF_01417

Sequences

Sequence LengthMass (Da)Tools
A9B9E6 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: C5FFB7B02F791188

FASTA64872,219
        10         20         30         40         50         60 
MSKSKPLTKK NDWSVEDSTV LYRLDKWGKD YFSINESGNI KVSPTGPEGD SLDLMVLVKE 

        70         80         90        100        110        120 
LNSRNLKSPL LLRFDDILED RIKKLHGAFK NAISHYEYEG EYKGVFPIKC NQQRHVVEEI 

       130        140        150        160        170        180 
VTCSREWHFG LEAGSKAELL IALSLLDDPE ALLICNGYKD KRYIETSILA RQLGRKPIVV 

       190        200        210        220        230        240 
IEQLDEVDRI INATKKIGSA PFIGIRAKLS SQSSGRWSNS IGEKSKFGLS IPEISQAVQQ 

       250        260        270        280        290        300 
LKDAGLLKEL ILLHFHIGSQ INDIAVLKNA LQEASHIYIE LKRLGAPMGH LDVGGGLGID 

       310        320        330        340        350        360 
YDGSRTATQA STNYSLQNYA NDVVATIQEC CKENQVQVPT LVSENGRAVS SHFSILVFNV 

       370        380        390        400        410        420 
LGTSSIPSDT RATTEHECLS VQNLRQTLRS LSEEPHNIGV DISRLQEAWN DALKFKEDAL 

       430        440        450        460        470        480 
AAFRLGYIGL EERAKAEQLT WACAKALAVK LPKDTLIPEE LNALNAALAE TYYANISIFR 

       490        500        510        520        530        540 
SAPDTWAIGQ LFPIMPIHRL NEKPTQLGHF ADLTCDSDGK LSKFIDNGQA KSLIELHRLN 

       550        560        570        580        590        600 
SNEDYLIGMF LGGAYQEVMG NLHNLFGSTN SIHIRMAKNG GYKLDHVIRG DTKAEVLNAM 

       610        620        630        640 
EHDSEQLLER LRIASESAIQ QGKLKINDAQ RLIEHVETSL RQSTYLQE

« 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		CP000878 Genomic DNA. Translation: ABX07983.1.
RefSeqYP_001549937.1. NC_009976.1.

3D structure databases

ProteinModelPortalA9B9E6.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9B9E6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5730160.
GenomeReviewsGene locus P9211_00521 in contig CP000878_GR.
KEGGpmj:P9211_00521.
PATRIC22985510. VBIProMar136502_0054.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG321436.
OMALICNGYK.
PhylomeDBA9B9E6.
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.
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.
SUPFAMSSF50621. Racem_decarbox_C. 1 hit.
TIGRFAMsTIGR01273. SpeA. 1 hit.
PROSITEPS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA9B9E6_PROM4
AccessionPrimary (citable) accession number: A9B9E6
Entry history
Integrated into UniProtKB/TrEMBL: January 15, 2008
Last sequence update: January 15, 2008
Last modified: December 14, 2011
This is version 24 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