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P21170

- SPEA_ECOLI

UniProt

P21170 - SPEA_ECOLI

Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (29 Aug 2003)
      Previous versions | rss
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    Functioni

    Catalyzes the biosynthesis of agmatine from arginine.By similarity

    Catalytic activityi

    L-arginine = agmatine + CO2.

    Cofactori

    Pyridoxal phosphate.
    Magnesium.

    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. spermidine biosynthetic process Source: UniProtKB-HAMAP

    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

    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 – 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.
    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.
    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

    Experimental Info

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

    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

    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: October 1, 2014
    This is version 134 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