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P21170

- SPEA_ECOLI

UniProt

P21170 - SPEA_ECOLI

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Protein

Biosynthetic arginine decarboxylase

Gene
speA, b2938, JW2905
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

L-arginine = agmatine + CO2.UniRule annotation

Cofactori

Pyridoxal phosphate.
Magnesium.

pH dependencei

Optimum pH is 8.4.UniRule annotation

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. 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.
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: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10959. speA.

Subcellular locationi

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 decarboxylaseUniRule annotationPRO_0000149960Add
BLAST

Amino acid modifications

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

Post-translational modificationi

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

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.UniRule annotation

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NZQX-ray3.10A/B1-658[»]
ProteinModelPortaliP21170.
SMRiP21170. Positions 34-658.

Miscellaneous databases

EvolutionaryTraceiP21170.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni307 – 31711Substrate-binding Reviewed predictionAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
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

MSDDMSMGLP SSAGEHGVLR SMQEVAMSSQ EASKMLRTYN IAWWGNNYYD    50
VNELGHISVC PDPDVPEARV DLAQLVKTRE AQGQRLPALF CFPQILQHRL 100
RSINAAFKRA RESYGYNGDY FLVYPIKVNQ HRRVIESLIH SGEPLGLEAG 150
SKAELMAVLA HAGMTRSVIV CNGYKDREYI RLALIGEKMG HKVYLVIEKM 200
SEIAIVLDEA ERLNVVPRLG VRARLASQGS GKWQSSGGEK SKFGLAATQV 250
LQLVETLREA GRLDSLQLLH FHLGSQMANI RDIATGVRES ARFYVELHKL 300
GVNIQCFDVG GGLGVDYEGT RSQSDCSVNY GLNEYANNII WAIGDACEEN 350
GLPHPTVITE SGRAVTAHHT VLVSNIIGVE RNEYTVPTAP AEDAPRALQS 400
MWETWQEMHE PGTRRSLREW LHDSQMDLHD IHIGYSSGIF SLQERAWAEQ 450
LYLSMCHEVQ KQLDPQNRAH RPIIDELQER MADKMYVNFS LFQSMPDAWG 500
IDQLFPVLPL EGLDQVPERR AVLLDITCDS DGAIDHYIDG DGIATTMPMP 550
EYDPENPPML GFFMVGAYQE ILGNMHNLFG DTEAVDVFVF PDGSVEVELS 600
DEGDTVADML QYVQLDPKTL LTQFRDQVKK TDLDAELQQQ FLEEFEAGLY 650
GYTYLEDE 658
Length:658
Mass (Da):73,898
Last modified:August 29, 2003 - v2
Checksum:i22613CEA5F957CC3
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti226 – 2261A → R in AAA24646. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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.
PIRi A65079.
RefSeqi NP_417413.1. NC_000913.3.
YP_491137.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3NZQ X-ray 3.10 A/B 1-658 [» ]
ProteinModelPortali P21170.
SMRi P21170. Positions 34-658.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10905N.
IntActi P21170. 16 interactions.
STRINGi 511145.b2938.

Proteomic databases

PaxDbi P21170.
PRIDEi P21170.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75975 ; AAC75975 ; b2938 .
BAE77001 ; BAE77001 ; BAE77001 .
GeneIDi 12933352.
947432.
KEGGi ecj:Y75_p2868.
eco:b2938.
PATRICi 32121288. VBIEscCol129921_3032.

Organism-specific databases

EchoBASEi EB0952.
EcoGenei EG10959. speA.

Phylogenomic databases

eggNOGi COG1166.
HOGENOMi HOG000029191.
KOi K01585.
OMAi IDHYVDG.
OrthoDBi EOG676Z0R.
PhylomeDBi P21170.

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .
BioCyci EcoCyc:ARGDECARBOXBIO-MONOMER.
ECOL316407:JW2905-MONOMER.
MetaCyc:ARGDECARBOXBIO-MONOMER.
SABIO-RK P21170.

Miscellaneous databases

EvolutionaryTracei P21170.
PROi P21170.

Gene expression databases

Genevestigatori P21170.

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

« 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: June 11, 2014
This is version 133 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

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