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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Pasteurella multocida (strain Pm70)
Status
Reviewed-Annotation score: Annotation score: 2 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

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. spermidine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Polyamine biosynthesis, Spermidine biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

BioCyciPMUL272843:GC8W-1435-MONOMER.

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:PM1382
OrganismiPasteurella multocida (strain Pm70)
Taxonomic identifieri272843 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella
ProteomesiUP000000809: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 644644Biosynthetic arginine decarboxylasePRO_0000149966Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei113 – 1131N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi272843.PM1382.

Structurei

3D structure databases

ProteinModelPortaliQ9CL60.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni293 – 30311Substrate-bindingUniRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
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.

Q9CL60-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEQVTLTSDG TSSVFAENTV REVCNINYWG MRYYNVDEKG DIFVCPDPDK
60 70 80 90 100
PQNRVSLAAL AEKVQREQGA HLPTLFCFPQ IIQHRLRSIN QAFKRAREDF
110 120 130 140 150
GYEGNYFLVY PIKVNQHRRI VESLISSGQP LGLEAGSKAE LMAVLAHAGI
160 170 180 190 200
TQTVIVCNGY KDREYVRFAL MGEKLGHKVY LVIEKLSEIQ LVLEEAAKLN
210 220 230 240 250
VKPRLGVRAR LASQGSGKWQ SSGGEKSKFG LSASQVLSLV QMLKEHECLD
260 270 280 290 300
CLQLLHFHLG SQLGNIRDVA TGVRESARFY VELHKLGVNI QCFDVGGGLG
310 320 330 340 350
VDYEGNRTQS DCSVNYGLNE YADTVVWGIG QACREHGLPH PTIITESGRG
360 370 380 390 400
VTAHHAVLVS NVIGVERYKF ETLAAPAKDA PSVLHSMWET WVDIQSSREK
410 420 430 440 450
RSLRSWIHES QFDLSDVHNQ YNVGLLNLEQ RAWAEQLYLN ICHEVGQLFN
460 470 480 490 500
EKHRSHRTII DELQERFADK LYVNFSLFQS LPDAWGIDQL FPVCPISNLN
510 520 530 540 550
QPVSRRAVLL DITCDSDGTI DHYIDGDGIT TTMPMPHYEE DNPPLLGFFM
560 570 580 590 600
VGAYQEILGN MHNLFGDTST VDVLVHEQDK AYIVDYDEGN TVADMLEYVY
610 620 630 640
LDPKKLLDRY REQIEHSNLP ASEAIQFLNE LEVGLNGYTY LEDE
Length:644
Mass (Da):72,707
Last modified:June 1, 2001 - v1
Checksum:iF6A7FEB0B8DE3D82
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004439 Genomic DNA. Translation: AAK03466.1.
RefSeqiNP_246321.1. NC_002663.1.

Genome annotation databases

EnsemblBacteriaiAAK03466; AAK03466; PM1382.
GeneIDi1244729.
KEGGipmu:PM1382.
PATRICi22872023. VBIPasMul88067_1394.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004439 Genomic DNA. Translation: AAK03466.1.
RefSeqiNP_246321.1. NC_002663.1.

3D structure databases

ProteinModelPortaliQ9CL60.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272843.PM1382.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK03466; AAK03466; PM1382.
GeneIDi1244729.
KEGGipmu:PM1382.
PATRICi22872023. VBIPasMul88067_1394.

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
KOiK01585.
OMAiIDHYVDG.
OrthoDBiEOG676Z0R.

Enzyme and pathway databases

BioCyciPMUL272843:GC8W-1435-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Pm70.

Entry informationi

Entry nameiSPEA_PASMU
AccessioniPrimary (citable) accession number: Q9CL60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: June 1, 2001
Last modified: January 7, 2015
This is version 78 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. 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.