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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the biosynthesis of agmatine from arginine.By similarity

Catalytic activityi

L-arginine = agmatine + CO2.

Cofactori

Protein has several cofactor binding sites:

Pathwayi: agmatine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes agmatine from L-arginine.
Proteins known to be involved in this subpathway in this organism are:
  1. Biosynthetic arginine decarboxylase (speA)
This subpathway is part of the pathway agmatine biosynthesis, which is itself part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes agmatine from L-arginine, the pathway agmatine biosynthesis and in Amine and polyamine biosynthesis.

GO - Molecular functioni

GO - Biological processi

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

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:c3524
OrganismiEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Taxonomic identifieri199310 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000001410 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001499611 – 658Biosynthetic arginine decarboxylaseAdd BLAST658

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei127N6-(pyridoxal phosphate)lysineBy similarity1

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi199310.c3524.

Structurei

3D structure databases

ProteinModelPortaliQ8FE34.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni307 – 317Substrate-bindingSequence analysisAdd BLAST11

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105DP5. Bacteria.
COG1166. LUCA.
HOGENOMiHOG000029191.
KOiK01585.
OMAiDQLFPIM.

Family and domain databases

CDDicd06830. PLPDE_III_ADC. 1 hit.
Gene3Di2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
HAMAPiMF_01417. SpeA. 1 hit.
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]
PANTHERiPTHR11482:SF36. PTHR11482:SF36. 2 hits.
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.

Q8FE34-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDDMSMGLP SSAGEHGVLR SMQEVAMSSQ EASKMLRTYN IAWWGNNYYD
60 70 80 90 100
VNELGHISVC PDPDVPEARV DLAQLVKTRE AQGQRLPALF CFPQILQHRL
110 120 130 140 150
RSINAAFKRA RESYGYNGDY FLVYPIKVNQ HRRVIESLIH SGEPLGLEAG
160 170 180 190 200
SKAELMAVLA HAGMTRSVIV CNGYKDREYI RLALIGEKMG HKVYLVIEKM
210 220 230 240 250
SEIAIVLDEA ERLNVVPRLG VRARLASQGS GKWQSSGGEK SKFGLAATQV
260 270 280 290 300
LQLVETLREA GRLDSLQLLH FHLGSQMANI RDIATGVRES ARFYVELHKL
310 320 330 340 350
GVNIQCFDVG GGLGVDYEGT RSQSDCSVNY GLNEYANNII WAIGDACEEN
360 370 380 390 400
GLPHPTVITE SGRAVTAHHT VLVSNIIGVE RNEYTVPTAP AEDAPRALQS
410 420 430 440 450
MWETWQEMHE PGTRRSLREW LHDSQMDLHD IHIGYSSGTF SLQERAWAEQ
460 470 480 490 500
LYLSMCHEVQ KQLDPQNRAH RPIIDELQER MADKMYVNFS LFQSMPDAWG
510 520 530 540 550
IDQLFPVLPL EGLDQVPERR AVLLDITCDS DGAIDHYIDG DGIATTMPMP
560 570 580 590 600
EYDPENPPML GFFMVGAYQE ILGNMHNLFG DTEAVDVFVF PDGSVEVELS
610 620 630 640 650
DEGDTVADML QYVQLDPKTL LTQFRDQVKK TDLDAELQQQ FLEEFEAGLY

GYTYLEDE
Length:658
Mass (Da):73,886
Last modified:March 29, 2004 - v2
Checksum:i87106BF8727B6EE2
GO

Sequence cautioni

The sequence AAN81972 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014075 Genomic DNA. Translation: AAN81972.1. Different initiation.
RefSeqiWP_001295380.1. NC_004431.1.

Genome annotation databases

EnsemblBacteriaiAAN81972; AAN81972; c3524.
KEGGiecc:c3524.
PATRICi18284870. VBIEscCol75197_3320.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014075 Genomic DNA. Translation: AAN81972.1. Different initiation.
RefSeqiWP_001295380.1. NC_004431.1.

3D structure databases

ProteinModelPortaliQ8FE34.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi199310.c3524.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN81972; AAN81972; c3524.
KEGGiecc:c3524.
PATRICi18284870. VBIEscCol75197_3320.

Phylogenomic databases

eggNOGiENOG4105DP5. Bacteria.
COG1166. LUCA.
HOGENOMiHOG000029191.
KOiK01585.
OMAiDQLFPIM.

Enzyme and pathway databases

UniPathwayiUPA00186; UER00284.

Family and domain databases

CDDicd06830. PLPDE_III_ADC. 1 hit.
Gene3Di2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
HAMAPiMF_01417. SpeA. 1 hit.
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]
PANTHERiPTHR11482:SF36. PTHR11482:SF36. 2 hits.
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...

Entry informationi

Entry nameiSPEA_ECOL6
AccessioniPrimary (citable) accession number: Q8FE34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: March 29, 2004
Last modified: November 2, 2016
This is version 90 of the entry and version 2 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

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 one 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.