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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the biosynthesis of agmatine from arginine.UniRule annotation

Catalytic activityi

L-arginine = agmatine + CO2.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotation
  • pyridoxal 5'-phosphateUniRule annotation

Pathwayi

GO - Molecular functioni

  1. arginine decarboxylase activity Source: UniProtKB-HAMAP
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. arginine catabolic process Source: InterPro
  2. putrescine biosynthetic process Source: UniProtKB-HAMAP
  3. spermidine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Polyamine biosynthesis, Putrescine biosynthesis, Spermidine biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

BioCyciHDEF572265:GJAB-1543-MONOMER.
UniPathwayiUPA00186; UER00284.

Names & Taxonomyi

Protein namesi
Recommended name:
Biosynthetic arginine decarboxylaseUniRule annotation (EC:4.1.1.19UniRule annotation)
Short name:
ADCUniRule annotation
Gene namesi
Name:speAUniRule annotation
Ordered Locus Names:HDEF_1524
OrganismiHamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT)
Taxonomic identifieri572265 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeaphid secondary symbiontsCandidatus Hamiltonella
ProteomesiUP000002334 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 633633Biosynthetic arginine decarboxylasePRO_1000215248Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei102 – 1021N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi572265.HDEF_1524.

Structurei

3D structure databases

ProteinModelPortaliC4K6F4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni282 – 29211Substrate-bindingUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG1166.
KOiK01585.
OMAiIDHYVDG.
OrthoDBiEOG676Z0R.

Family and domain databases

Gene3Di2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
HAMAPiMF_01417. SpeA.
InterProiIPR009006. 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]
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PIRSFiPIRSF001336. Arg_decrbxlase. 1 hit.
PRINTSiPR01180. ARGDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR01273. speA. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C4K6F4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNDRHAEKIR RAYNVAYWGN DYFYINDLGH ICVRPNPEVS QSSIDLAELL
60 70 80 90 100
KEKEGKNPQP LPALFFFPQI LQHRLHAINK AFKSARDSFG YQGDYCLVYP
110 120 130 140 150
IKVNQHRRVI ESLLKSGESL GLEAGSKAEM VAVLAYAGGT RSLIVCNGYK
160 170 180 190 200
DREYIRLALM GEKLGYKVYL VIEKMSEIKM VLEEAKRLNV VPRLGVRARL
210 220 230 240 250
ASEGSGKWQA SGGEKSKFGL SATQVLQLVE ILKSADCLSG LQLLHFHLGS
260 270 280 290 300
QLSNIHDIAT GVRESARFYV ELHKLGVKIS CFDVGGGLGV DYEGTRSQSD
310 320 330 340 350
CSVNYGLKEY ANNVIWGIGE ICNENHLPHP TVISESGRAL TAHHTVLISN
360 370 380 390 400
VIGVERNEFS PPQAPEKHSP RALESLWYTW QEMQKPDHRH SLRECLHDSQ
410 420 430 440 450
RDLQDVHTQY THGILDLKQR AWAEQLYLQI CHHIQKELDP SDRAHRTMID
460 470 480 490 500
NLQERMADKL YVNFSLFQSL PDAWGINQLF PILPLEGLNQ RPERRAVLLD
510 520 530 540 550
ITCDSDGIIE HYVDGDGVAN TLPIPPYDAE NPPILGFFMV GAYQEILGNM
560 570 580 590 600
HNLFGDTAVV EVSLDEQEKI SVKIDNPGNT VSDMLKYVKL DPKALLAYFA
610 620 630
QKIKKTDLNA QLQMAFLEEF EASLYGYTYL EHD
Length:633
Mass (Da):71,505
Last modified:July 6, 2009 - v1
Checksum:i444A0217E53529B2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001277 Genomic DNA. Translation: ACQ68147.1.
RefSeqiYP_002924295.1. NC_012751.1.

Genome annotation databases

EnsemblBacteriaiACQ68147; ACQ68147; HDEF_1524.
GeneIDi7951124.
KEGGihde:HDEF_1524.
PATRICi31974509. VBICanHam112931_1522.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001277 Genomic DNA. Translation: ACQ68147.1.
RefSeqiYP_002924295.1. NC_012751.1.

3D structure databases

ProteinModelPortaliC4K6F4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi572265.HDEF_1524.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACQ68147; ACQ68147; HDEF_1524.
GeneIDi7951124.
KEGGihde:HDEF_1524.
PATRICi31974509. VBICanHam112931_1522.

Phylogenomic databases

eggNOGiCOG1166.
KOiK01585.
OMAiIDHYVDG.
OrthoDBiEOG676Z0R.

Enzyme and pathway databases

UniPathwayiUPA00186; UER00284.
BioCyciHDEF572265:GJAB-1543-MONOMER.

Family and domain databases

Gene3Di2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
HAMAPiMF_01417. SpeA.
InterProiIPR009006. 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]
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PIRSFiPIRSF001336. Arg_decrbxlase. 1 hit.
PRINTSiPR01180. ARGDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR01273. speA. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Hamiltonella defensa, genome evolution of protective bacterial endosymbiont from pathogenic ancestors."
    Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.
    Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 5AT.

Entry informationi

Entry nameiSPEA_HAMD5
AccessioniPrimary (citable) accession number: C4K6F4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2009
Last sequence update: July 6, 2009
Last modified: February 3, 2015
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.