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C1D018 (C1D018_DEIDV) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 19. 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 EMBL ACO45270.1
Ordered Locus Names:Deide_04410
OrganismDeinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923) [Complete proteome] [HAMAP]
Taxonomic identifier546414 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

Protein attributes

Sequence length640 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 RuleBase RU003740 SAAS SAAS009006

Cofactor

Magnesium By similarity. HAMAP MF_01417 RuleBase RU003740 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
C1D018 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: A2DBDAABAC951CAF

FASTA64071,266
        10         20         30         40         50         60 
MTTTPTPGFT TADAAELYQV PNWSGGWFRV SDKGQLEATT SPGLHVPLRA IVDEIVDRGE 

        70         80         90        100        110        120 
SLPVILRFPQ VLAGRVKHLN EVFGQAIAEY GYTRHYQGVF PIKVNQRRAV VETVASAGYD 

       130        140        150        160        170        180 
YAHGLEAGSK AELALCLAQR MHPDALLCCN GFKDDGFIKL ALWGRTLGKN VVITIEKFSE 

       190        200        210        220        230        240 
LDRILKQAKA LGVRPAIGVR FKLHARGSGQ WEESGGDQAK FGLNAYELLR VVERLKEEGM 

       250        260        270        280        290        300 
IDSLVMLHTH IGSQITDIRR VKVAVREATQ TYAGLIAAGA ELKYLNVGGG LGVDYDGSKT 

       310        320        330        340        350        360 
TFYASMNYTV KEYAADVVYT IQETCKARGV PEPIIISESG RALTAHHAVL ILPVIDVTGP 

       370        380        390        400        410        420 
TRNLEDQELV APAEDSHQLI KDMHEIVQNI SMRNYREMYN DAVGDKQTLH DLFDLGYVTL 

       430        440        450        460        470        480 
QDRARGEALF NAILRKISKL IQSEKYVPDE LEDLQKVLAD KYICNFSLFQ SLPDNWAIQA 

       490        500        510        520        530        540 
LFPIVPLDRL NQKPTRQATL VDITCDSDGK IEKFIDLRDV KATLPLHEPG KQPYYLGVFL 

       550        560        570        580        590        600 
MGAYQDVLGS SHNLFGKVSE AHVTVRPGGR FNIDLFVRGQ KARRMIESMG YEEPMLRDSI 

       610        620        630        640 
EDQADAALKV GTLTPGQEHE LLEDYGEELL GYTYLEYEES

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References

[1]"Alliance of proteomics and genomics to unravel the specificities of Sahara bacterium Deinococcus deserti."
de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B., Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M., Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.
PLoS Genet. 5:E1000434-E1000434(2009) [PubMed: 19370165] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VCD115 / DSM 17065 / LMG 22923.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001114 Genomic DNA. Translation: ACO45270.1.
RefSeqYP_002785024.1. NC_012526.1.

3D structure databases

ProteinModelPortalC1D018.
ModBaseSearch...

Protein-protein interaction databases

STRINGC1D018.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7737967.
GenomeReviewsGene locus Deide_04410 in contig CP001114_GR.
KEGGddr:Deide_04410.
PATRIC21614380. VBIDeiDes121019_0493.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMALICNGYK.
ProtClustDBPRK05354.

Family and domain databases

HAMAPMF_01417. SpeA.
[Tree]
InterProIPR009006. Ala_racemase/Decarboxylase_C.
IPR002985. Arg_decrbxlase.
IPR022643. De-COase2_C.
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.
SUPFAMSSF50621. Racem_decarbox_C. 1 hit.
TIGRFAMsTIGR01273. SpeA. 1 hit.
PROSITEPS00878. ODR_DC_2_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC1D018_DEIDV
AccessionPrimary (citable) accession number: C1D018
Entry history
Integrated into UniProtKB/TrEMBL: May 26, 2009
Last sequence update: May 26, 2009
Last modified: December 14, 2011
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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