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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

GO - Molecular functioni

  1. arginine decarboxylase activity Source: EcoCyc
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. arginine catabolic process Source: EcoCyc
  2. putrescine biosynthetic process Source: EcoCyc
  3. putrescine biosynthetic process from arginine Source: GO_Central
  4. 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10959. speA.

Subcellular locationi

  1. Periplasm 1 Publication

GO - Cellular componenti

  1. periplasmic space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 658658Biosynthetic arginine decarboxylasePRO_0000149960Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei127 – 1271N6-(pyridoxal phosphate)lysineBy similarity

Post-translational modificationi

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

Proteomic databases

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.

Gene expression databases

GenevestigatoriP21170.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

DIPiDIP-10905N.
IntActiP21170. 16 interactions.
STRINGi511145.b2938.

Structurei

Secondary structure

1
658
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni35 – 406Combined sources
Helixi41 – 444Combined sources
Turni45 – 484Combined sources
Beta strandi49 – 513Combined sources
Beta strandi55 – 595Combined sources
Helixi72 – 8110Combined sources
Beta strandi86 – 916Combined sources
Helixi93 – 11422Combined sources
Beta strandi120 – 1256Combined sources
Helixi126 – 1283Combined sources
Helixi132 – 1398Combined sources
Beta strandi141 – 1433Combined sources
Beta strandi145 – 1517Combined sources
Helixi152 – 16211Combined sources
Beta strandi168 – 1714Combined sources
Helixi177 – 18812Combined sources
Beta strandi192 – 1976Combined sources
Helixi200 – 21213Combined sources
Beta strandi219 – 2235Combined sources
Beta strandi226 – 2283Combined sources
Beta strandi235 – 2395Combined sources
Helixi247 – 25913Combined sources
Turni263 – 2653Combined sources
Beta strandi266 – 2705Combined sources
Helixi280 – 29819Combined sources
Turni299 – 3013Combined sources
Beta strandi306 – 3083Combined sources
Beta strandi317 – 3204Combined sources
Beta strandi322 – 3243Combined sources
Helixi332 – 35019Combined sources
Beta strandi356 – 3594Combined sources
Helixi362 – 3665Combined sources
Beta strandi369 – 38012Combined sources
Helixi396 – 40813Combined sources
Beta strandi409 – 4124Combined sources
Helixi417 – 43620Combined sources
Helixi442 – 46221Combined sources
Helixi468 – 4703Combined sources
Helixi471 – 4799Combined sources
Beta strandi483 – 4897Combined sources
Helixi491 – 4944Combined sources
Helixi497 – 5004Combined sources
Beta strandi507 – 5115Combined sources
Beta strandi519 – 5268Combined sources
Beta strandi537 – 5393Combined sources
Beta strandi542 – 5498Combined sources
Beta strandi559 – 5624Combined sources
Helixi570 – 5723Combined sources
Beta strandi583 – 5897Combined sources
Beta strandi595 – 6017Combined sources
Helixi606 – 6127Combined sources
Helixi617 – 62711Combined sources
Helixi629 – 6313Combined sources
Helixi635 – 64915Combined sources
Beta strandi650 – 6545Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NZQX-ray3.10A/B1-658[»]
ProteinModelPortaliP21170.
SMRiP21170. Positions 34-658.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21170.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni307 – 31711Substrate-bindingSequence AnalysisAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
InParanoidiP21170.
KOiK01585.
OMAiIDHYVDG.
OrthoDBiEOG676Z0R.
PhylomeDBiP21170.

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti226 – 2261A → R in AAA24646 (PubMed:2198270).Curated

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.
YP_491137.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75975; AAC75975; b2938.
BAE77001; BAE77001; BAE77001.
GeneIDi12933352.
947432.
KEGGiecj:Y75_p2868.
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.
YP_491137.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NZQX-ray3.10A/B1-658[»]
ProteinModelPortaliP21170.
SMRiP21170. Positions 34-658.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10905N.
IntActiP21170. 16 interactions.
STRINGi511145.b2938.

Proteomic databases

PaxDbiP21170.
PRIDEiP21170.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75975; AAC75975; b2938.
BAE77001; BAE77001; BAE77001.
GeneIDi12933352.
947432.
KEGGiecj:Y75_p2868.
eco:b2938.
PATRICi32121288. VBIEscCol129921_3032.

Organism-specific databases

EchoBASEiEB0952.
EcoGeneiEG10959. speA.

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
InParanoidiP21170.
KOiK01585.
OMAiIDHYVDG.
OrthoDBiEOG676Z0R.
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.

Gene expression databases

GenevestigatoriP21170.

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

« Hide 'large scale' publications
  1. "Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli."
    Moore R.C., Boyle S.M.
    J. Bacteriol. 172:4631-4640(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING.
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Influence of cyclic AMP, agmatine, and a novel protein encoded by a flanking gene on speB (agmatine ureohydrolase) in Escherichia coli."
    Szumanski M.B.W., Boyle S.M.
    J. Bacteriol. 174:758-764(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 635-658.
    Strain: K12.
  5. "Biosynthetic arginine decarboxylase from Escherichia coli. Purification and properties."
    Wu W.H., Morris D.R.
    J. Biol. Chem. 248:1687-1695(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: UW 44 / ATCC 27549.

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: April 29, 2015
This is version 139 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

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.