Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

B5YQD6

- SPEA_ECO5E

UniProt

B5YQD6 - SPEA_ECO5E

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Escherichia coli O157:H7 (strain EC4115 / EHEC)
Status
Reviewed - 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

BioCyciECOL444450:GHOB-4228-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:ECH74115_4241
OrganismiEscherichia coli O157:H7 (strain EC4115 / EHEC)
Taxonomic identifieri444450 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001737: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 632632Biosynthetic arginine decarboxylasePRO_1000145592Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei101 – 1011N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi444450.ECH74115_4241.

Structurei

3D structure databases

ProteinModelPortaliB5YQD6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni281 – 29111Substrate-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.

B5YQD6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSQEASKML RTYNIAWWGN NYYDVNELGH ISVCPDPDVP EARVDLAQLV
60 70 80 90 100
KTREAQGQRL PALFCFPQIL QHRLRSINAA FKRARESYGY NGDYFLVYPI
110 120 130 140 150
KVNQHRRVIE SLIHSGEPLG LEAGSKAELM AVLAHAGMTR SVIVCNGYKD
160 170 180 190 200
REYIRLALIG EKMGHKVYLV IEKMSEIAIV LDEAERLNVV PRLGVRARLA
210 220 230 240 250
SQGSGKWQSS GGEKSKFGLA ATQVLQLVET LREAGRLDSL QLLHFHLGSQ
260 270 280 290 300
MANIRDIATG VRESARFYVE LHKLGVNIQC FDVGGGLGVD YEGTRSQSDC
310 320 330 340 350
SVNYGLNEYA NNIIWAIGDA CEENGLPHPT VITESGRAVT AHHTVLVSNI
360 370 380 390 400
IGVERNEYTV PTAPAEDAPR ALQSMWETWQ EMHEPGTRRS LREWLHDSQM
410 420 430 440 450
DLHDIHIGYS SGTFSLQERA WAEQLYLSMC HEVQKQLDPQ NRAHRPIIDE
460 470 480 490 500
LQERMADKMY VNFSLFQSMP DAWGIDQLFP VLPLEGLDQV PERRAVLLDI
510 520 530 540 550
TCDSDGAIDH YIDGDGIATT MPMPEYDPEN PPMLGFFMVG AYQEILGNMH
560 570 580 590 600
NLFGDTEAVD VFVFPDGSVE VELSDEGDTV ADMLQYVQLD PKTLLTQFRD
610 620 630
QVKKTDLDAE LQQQFLEEFE AGLYGYTYLE DE
Length:632
Mass (Da):71,181
Last modified:November 25, 2008 - v1
Checksum:iEE36CC59AF9D2569
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001164 Genomic DNA. Translation: ACI37609.1.
RefSeqiYP_002272418.1. NC_011353.1.

Genome annotation databases

EnsemblBacteriaiACI37609; ACI37609; ECH74115_4241.
GeneIDi6968274.
KEGGiecf:ECH74115_4241.
PATRICi18369065. VBIEscCol74651_4159.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001164 Genomic DNA. Translation: ACI37609.1 .
RefSeqi YP_002272418.1. NC_011353.1.

3D structure databases

ProteinModelPortali B5YQD6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 444450.ECH74115_4241.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACI37609 ; ACI37609 ; ECH74115_4241 .
GeneIDi 6968274.
KEGGi ecf:ECH74115_4241.
PATRICi 18369065. VBIEscCol74651_4159.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .
BioCyci ECOL444450:GHOB-4228-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: EC4115 / EHEC.

Entry informationi

Entry nameiSPEA_ECO5E
AccessioniPrimary (citable) accession number: B5YQD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 25, 2008
Last modified: November 26, 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