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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the biosynthesis of agmatine from arginine.By similarity

Catalytic activityi

L-arginine = agmatine + CO2.

Cofactori

Protein has several cofactor binding sites:

pH dependencei

Optimum pH is 8.4.

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

  • arginine decarboxylase activity Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • arginine catabolic process Source: EcoCyc
  • putrescine biosynthetic process Source: EcoCyc
  • putrescine biosynthetic process from arginine Source: GO_Central
  • 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

BioCyciEcoCyc:ARGDECARBOXBIO-MONOMER.
ECOL316407:JW2905-MONOMER.
MetaCyc:ARGDECARBOXBIO-MONOMER.
BRENDAi4.1.1.19. 2026.
SABIO-RKP21170.
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:b2938, JW2905
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10959. speA.

Subcellular locationi

  • Periplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001499601 – 658Biosynthetic arginine decarboxylaseAdd BLAST658

Amino acid modifications

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

Post-translational modificationi

Processed post-translationally to a 70 kDa mature form.
The N-terminus is blocked.

Proteomic databases

EPDiP21170.
PaxDbiP21170.
PRIDEiP21170.

Expressioni

Inductioni

By growth in an acidic enriched medium containing arginine (biodegradative form), by growth in minimal media at neutral pH (biosynthetic). Putrescine and spermidine repress the speA gene and feedback inhibit ADC.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi4262346. 11 interactors.
DIPiDIP-10905N.
IntActiP21170. 16 interactors.
STRINGi511145.b2938.

Structurei

Secondary structure

1658
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni35 – 40Combined sources6
Helixi41 – 44Combined sources4
Turni45 – 48Combined sources4
Beta strandi49 – 51Combined sources3
Beta strandi55 – 59Combined sources5
Helixi72 – 81Combined sources10
Beta strandi86 – 91Combined sources6
Helixi93 – 114Combined sources22
Beta strandi120 – 125Combined sources6
Helixi126 – 128Combined sources3
Helixi132 – 139Combined sources8
Beta strandi141 – 143Combined sources3
Beta strandi145 – 151Combined sources7
Helixi152 – 162Combined sources11
Beta strandi168 – 171Combined sources4
Helixi177 – 188Combined sources12
Beta strandi192 – 197Combined sources6
Helixi200 – 212Combined sources13
Beta strandi219 – 223Combined sources5
Beta strandi226 – 228Combined sources3
Beta strandi235 – 239Combined sources5
Helixi247 – 259Combined sources13
Turni263 – 265Combined sources3
Beta strandi266 – 270Combined sources5
Helixi280 – 298Combined sources19
Turni299 – 301Combined sources3
Beta strandi306 – 308Combined sources3
Beta strandi317 – 320Combined sources4
Beta strandi322 – 324Combined sources3
Helixi332 – 350Combined sources19
Beta strandi356 – 359Combined sources4
Helixi362 – 366Combined sources5
Beta strandi369 – 380Combined sources12
Helixi396 – 408Combined sources13
Beta strandi409 – 412Combined sources4
Helixi417 – 436Combined sources20
Helixi442 – 462Combined sources21
Helixi468 – 470Combined sources3
Helixi471 – 479Combined sources9
Beta strandi483 – 489Combined sources7
Helixi491 – 494Combined sources4
Helixi497 – 500Combined sources4
Beta strandi507 – 511Combined sources5
Beta strandi519 – 526Combined sources8
Beta strandi537 – 539Combined sources3
Beta strandi542 – 549Combined sources8
Beta strandi559 – 562Combined sources4
Helixi570 – 572Combined sources3
Beta strandi583 – 589Combined sources7
Beta strandi595 – 601Combined sources7
Helixi606 – 612Combined sources7
Helixi617 – 627Combined sources11
Helixi629 – 631Combined sources3
Helixi635 – 649Combined sources15
Beta strandi650 – 654Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NZQX-ray3.10A/B1-658[»]
ProteinModelPortaliP21170.
SMRiP21170.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21170.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105DP5. Bacteria.
COG1166. LUCA.
HOGENOMiHOG000029191.
InParanoidiP21170.
KOiK01585.
OMAiDQLFPIM.
PhylomeDBiP21170.

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.

P21170-1 [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 IHIGYSSGIF 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):73,898
Last modified:August 29, 2003 - v2
Checksum:i22613CEA5F957CC3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti226A → R in AAA24646 (PubMed:2198270).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31770 Genomic DNA. Translation: AAA24646.1.
U28377 Genomic DNA. Translation: AAA69105.1.
U00096 Genomic DNA. Translation: AAC75975.1.
AP009048 Genomic DNA. Translation: BAE77001.1.
M32363 Genomic DNA. No translation available.
PIRiA65079.
RefSeqiNP_417413.1. NC_000913.3.
WP_001300904.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75975; AAC75975; b2938.
BAE77001; BAE77001; BAE77001.
GeneIDi947432.
KEGGiecj:JW2905.
eco:b2938.
PATRICi32121288. VBIEscCol129921_3032.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31770 Genomic DNA. Translation: AAA24646.1.
U28377 Genomic DNA. Translation: AAA69105.1.
U00096 Genomic DNA. Translation: AAC75975.1.
AP009048 Genomic DNA. Translation: BAE77001.1.
M32363 Genomic DNA. No translation available.
PIRiA65079.
RefSeqiNP_417413.1. NC_000913.3.
WP_001300904.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NZQX-ray3.10A/B1-658[»]
ProteinModelPortaliP21170.
SMRiP21170.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262346. 11 interactors.
DIPiDIP-10905N.
IntActiP21170. 16 interactors.
STRINGi511145.b2938.

Proteomic databases

EPDiP21170.
PaxDbiP21170.
PRIDEiP21170.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75975; AAC75975; b2938.
BAE77001; BAE77001; BAE77001.
GeneIDi947432.
KEGGiecj:JW2905.
eco:b2938.
PATRICi32121288. VBIEscCol129921_3032.

Organism-specific databases

EchoBASEiEB0952.
EcoGeneiEG10959. speA.

Phylogenomic databases

eggNOGiENOG4105DP5. Bacteria.
COG1166. LUCA.
HOGENOMiHOG000029191.
InParanoidiP21170.
KOiK01585.
OMAiDQLFPIM.
PhylomeDBiP21170.

Enzyme and pathway databases

UniPathwayiUPA00186; UER00284.
BioCyciEcoCyc:ARGDECARBOXBIO-MONOMER.
ECOL316407:JW2905-MONOMER.
MetaCyc:ARGDECARBOXBIO-MONOMER.
BRENDAi4.1.1.19. 2026.
SABIO-RKP21170.

Miscellaneous databases

EvolutionaryTraceiP21170.
PROiP21170.

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_ECOLI
AccessioniPrimary (citable) accession number: P21170
Secondary accession number(s): Q2M9Q5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: August 29, 2003
Last modified: November 2, 2016
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

ADC can be found in two forms: biodegradative and biosynthetic. The biodegradative form may play a role in regulating pH by consuming proteins.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.