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B1LDE8

- SPEA_ECOSM

UniProt

B1LDE8 - SPEA_ECOSM

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Protein

Biosynthetic arginine decarboxylase

Gene
speA, EcSMS35_3081
Organism
Escherichia coli (strain SMS-3-5 / SECEC)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the biosynthesis of agmatine from arginine By similarity.UniRule annotation

Catalytic activityi

L-arginine = agmatine + CO2.UniRule annotation

Cofactori

Magnesium By similarity.UniRule annotation
Pyridoxal phosphate By similarity.UniRule 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

BioCyciECOL439855:GHHB-3078-MONOMER.
UniPathwayiUPA00186; UER00284.

Names & Taxonomyi

Protein namesi
Recommended name:
Biosynthetic arginine decarboxylase (EC:4.1.1.19)
Short name:
ADC
Gene namesi
Name:speA
Ordered Locus Names:EcSMS35_3081
OrganismiEscherichia coli (strain SMS-3-5 / SECEC)
Taxonomic identifieri439855 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000007011: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 632632Biosynthetic arginine decarboxylaseUniRule annotationPRO_1000145593Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei101 – 1011N6-(pyridoxal phosphate)lysine By similarity

Interactioni

Protein-protein interaction databases

STRINGi439855.EcSMS35_3081.

Structurei

3D structure databases

ProteinModelPortaliB1LDE8.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni281 – 29111Substrate-binding Reviewed predictionAdd
BLAST

Sequence similaritiesi

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.

B1LDE8-1 [UniParc]FASTAAdd to Basket

« Hide

MSSQEASKML RTYNIAWWGN NYYDVNELGH ISVCPDPDVP EARVDLAQLV    50
KTREAQGQRL PALFCFPQIL QHRLRSINAA FKRARESYGY NGDYFLVYPI 100
KVNQHRRVIE SLIHSGEPLG LEAGSKAELM AVLAHAGMTR SVIVCNGYKD 150
REYIRLALIG EKMGHKVYLV IEKMSEIAIV LDEAERLNVV PRLGVRARLA 200
SQGSGKWQSS GGEKSKFGLA ATQVLQLVET LREAGRLDSL QLLHFHLGSQ 250
MANIRDIATG VRESARFYVE LHKLGVNIQC FDVGGGLGVD YEGTRSQSDC 300
SVNYGLNEYA NNIIWAIGDA CEENGLPHPT VITESGRAVT AHHTVLVSNI 350
IGVERNEYTV PTAPAEDAPR ALQSMWETWQ EMHEPGTRRS LREWLHDSQM 400
DLHDIHIGYS SGTFSLQERA WAEQLYLSMC HEVQKQLDPQ NRAHRPIIDE 450
LQERMADKMY VNFSLFQSMP DAWGIDQLFP VLPLEGLDQV PERRAVLLDI 500
TCDSDGAIDH YIDGDGIATT MPMPEYDPEN PPMLGFFMVG AYQEILGNMH 550
NLFGDTEAVD VFVFPDGSVE VELSDEGDTV ADMLQYVQLD PKTLLTQFRD 600
QVKKTDLDAE LQQQFLEEFE AGLYGYTYLE DE 632
Length:632
Mass (Da):71,181
Last modified:April 29, 2008 - v1
Checksum:iEE36CC59AF9D2569
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000970 Genomic DNA. Translation: ACB15562.1.
RefSeqiYP_001745100.1. NC_010498.1.

Genome annotation databases

EnsemblBacteriaiACB15562; ACB15562; EcSMS35_3081.
GeneIDi6142594.
KEGGiecm:EcSMS35_3081.
PATRICi18435078. VBIEscCol6161_3234.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000970 Genomic DNA. Translation: ACB15562.1 .
RefSeqi YP_001745100.1. NC_010498.1.

3D structure databases

ProteinModelPortali B1LDE8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 439855.EcSMS35_3081.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACB15562 ; ACB15562 ; EcSMS35_3081 .
GeneIDi 6142594.
KEGGi ecm:EcSMS35_3081.
PATRICi 18435078. VBIEscCol6161_3234.

Phylogenomic databases

eggNOGi COG1166.
HOGENOMi HOG000029191.
KOi K01585.
OMAi IDHYVDG.
OrthoDBi EOG676Z0R.

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .
BioCyci ECOL439855:GHHB-3078-MONOMER.

Family and domain databases

Gene3Di 2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
HAMAPi MF_01417. SpeA.
InterProi IPR009006. 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 ]
Pfami PF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view ]
PIRSFi PIRSF001336. Arg_decrbxlase. 1 hit.
PRINTSi PR01180. ARGDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMi SSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsi TIGR01273. speA. 1 hit.
PROSITEi PS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Insights into the environmental resistance gene pool from the genome sequence of the multidrug-resistant environmental isolate Escherichia coli SMS-3-5."
    Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R.
    J. Bacteriol. 190:6779-6794(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SMS-3-5 / SECEC.

Entry informationi

Entry nameiSPEA_ECOSM
AccessioniPrimary (citable) accession number: B1LDE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: June 11, 2014
This is version 48 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

Documents

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

External Data

Dasty 3

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