Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P28629

- ADIA_ECOLI

UniProt

P28629 - ADIA_ECOLI

Protein

Biodegradative arginine decarboxylase

Gene

adiA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

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

    Catalytic activityi

    L-arginine = agmatine + CO2.

    Cofactori

    Pyridoxal phosphate.

    GO - Molecular functioni

    1. arginine decarboxylase activity Source: EcoCyc
    2. pyridoxal phosphate binding Source: EcoCyc

    GO - Biological processi

    1. arginine catabolic process Source: EcoliWiki
    2. intracellular pH elevation Source: EcoCyc

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciEcoCyc:ARGDECARBOXDEG-MONOMER.
    ECOL316407:JW5731-MONOMER.
    MetaCyc:ARGDECARBOXDEG-MONOMER.
    BRENDAi4.1.1.19. 2026.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Biodegradative arginine decarboxylase (EC:4.1.1.19)
    Short name:
    ADC
    Gene namesi
    Name:adiA
    Synonyms:adi
    Ordered Locus Names:b4117, JW5731
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11501. adiA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 755755Biodegradative arginine decarboxylasePRO_0000201149Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei386 – 3861N6-(pyridoxal phosphate)lysine

    Proteomic databases

    PaxDbiP28629.
    PRIDEiP28629.

    Expressioni

    Inductioni

    Under conditions of acidic pH, anaerobiosis and rich medium.

    Gene expression databases

    GenevestigatoriP28629.

    Interactioni

    Subunit structurei

    Homodecamer.

    Protein-protein interaction databases

    DIPiDIP-2903N.
    IntActiP28629. 6 interactions.
    MINTiMINT-1241522.
    STRINGi511145.b4117.

    Structurei

    Secondary structure

    1
    755
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65
    Helixi15 – 3016
    Beta strandi34 – 407
    Helixi41 – 488
    Turni49 – 513
    Beta strandi55 – 606
    Helixi66 – 8217
    Beta strandi88 – 925
    Helixi94 – 996
    Helixi103 – 1086
    Beta strandi110 – 1145
    Turni115 – 1173
    Helixi120 – 13617
    Helixi141 – 15010
    Beta strandi156 – 1605
    Turni161 – 1666
    Helixi167 – 1704
    Helixi172 – 18110
    Helixi183 – 1875
    Turni194 – 1974
    Turni200 – 2034
    Helixi205 – 21814
    Beta strandi221 – 2288
    Helixi229 – 24113
    Beta strandi247 – 2537
    Helixi256 – 26510
    Beta strandi268 – 2725
    Helixi287 – 2904
    Helixi292 – 30110
    Turni303 – 3053
    Helixi306 – 3083
    Beta strandi316 – 3216
    Beta strandi325 – 3284
    Helixi330 – 3378
    Turni338 – 3403
    Beta strandi342 – 3476
    Helixi354 – 3563
    Helixi358 – 3603
    Beta strandi363 – 3664
    Beta strandi374 – 38310
    Turni384 – 3863
    Beta strandi387 – 3893
    Beta strandi395 – 4006
    Helixi408 – 41710
    Helixi425 – 43814
    Helixi441 – 46929
    Turni470 – 4723
    Beta strandi477 – 4804
    Beta strandi482 – 4854
    Turni487 – 4893
    Beta strandi492 – 4943
    Helixi495 – 4973
    Helixi500 – 5056
    Helixi507 – 5093
    Turni517 – 5193
    Beta strandi528 – 5314
    Beta strandi535 – 5395
    Beta strandi547 – 5493
    Helixi556 – 5649
    Turni565 – 5673
    Beta strandi571 – 5733
    Beta strandi575 – 5817
    Turni588 – 5914
    Helixi592 – 60716
    Helixi611 – 6144
    Helixi616 – 6216
    Turni623 – 6253
    Helixi631 – 64515
    Helixi647 – 65610
    Beta strandi661 – 6633
    Helixi665 – 6739
    Beta strandi677 – 6815
    Helixi682 – 6843
    Beta strandi689 – 6924
    Beta strandi694 – 6963
    Turni697 – 6993
    Helixi716 – 73015
    Beta strandi741 – 7444
    Beta strandi747 – 7537

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VYCX-ray2.40A/B/C/D/E/F/G/H/I/J1-755[»]
    ProteinModelPortaliP28629.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP28629.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1982.
    HOGENOMiHOG000164394.
    KOiK01584.
    OMAiANDWVEC.
    OrthoDBiEOG696BRZ.
    PhylomeDBiP28629.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.100.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR005308. OKR_de-COase_N.
    IPR011193. Orn/lys/arg_de-COase.
    IPR000310. Orn/Lys/Arg_deCO2ase_major_dom.
    IPR008286. Prn/Lys/Arg_de-COase_C.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PfamiPF01276. OKR_DC_1. 1 hit.
    PF03711. OKR_DC_1_C. 1 hit.
    PF03709. OKR_DC_1_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF009393. Orn_decarb. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    SSF55904. SSF55904. 1 hit.
    PROSITEiPS00703. OKR_DC_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P28629-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKVLIVESEF LHQDTWVGNA VERLADALSQ QNVTVIKSTS FDDGFAILSS    50
    NEAIDCLMFS YQMEHPDEHQ NVRQLIGKLH ERQQNVPVFL LGDREKALAA 100
    MDRDLLELVD EFAWILEDTA DFIAGRAVAA MTRYRQQLLP PLFSALMKYS 150
    DIHEYSWAAP GHQGGVGFTK TPAGRFYHDY YGENLFRTDM GIERTSLGSL 200
    LDHTGAFGES EKYAARVFGA DRSWSVVVGT SGSNRTIMQA CMTDNDVVVV 250
    DRNCHKSIEQ GLMLTGAKPV YMVPSRNRYG IIGPIYPQEM QPETLQKKIS 300
    ESPLTKDKAG QKPSYCVVTN CTYDGVCYNA KEAQDLLEKT SDRLHFDEAW 350
    YGYARFNPIY ADHYAMRGEP GDHNGPTVFA THSTHKLLNA LSQASYIHVR 400
    EGRGAINFSR FNQAYMMHAT TSPLYAICAS NDVAVSMMDG NSGLSLTQEV 450
    IDEAVDFRQA MARLYKEFTA DGSWFFKPWN KEVVTDPQTG KTYDFADAPT 500
    KLLTTVQDCW VMHPGESWHG FKDIPDNWSM LDPIKVSILA PGMGEDGELE 550
    ETGVPAALVT AWLGRHGIVP TRTTDFQIMF LFSMGVTRGK WGTLVNTLCS 600
    FKRHYDANTP LAQVMPELVE QYPDTYANMG IHDLGDTMFA WLKENNPGAR 650
    LNEAYSGLPV AEVTPREAYN AIVDNNVELV SIENLPGRIA ANSVIPYPPG 700
    IPMLLSGENF GDKNSPQVSY LRSLQSWDHH FPGFEHETEG TEIIDGIYHV 750
    MCVKA 755
    Length:755
    Mass (Da):84,425
    Last modified:December 1, 1992 - v1
    Checksum:i0FCB715144649F8F
    GO

    Sequence cautioni

    The sequence AAA97017.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAE78119.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti75 – 751L → P(PubMed:2830169)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93362 Genomic DNA. Translation: AAA23481.1.
    U14003 Genomic DNA. Translation: AAA97017.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC77078.2.
    AP009048 Genomic DNA. Translation: BAE78119.1. Different initiation.
    M18425 Genomic DNA. No translation available.
    PIRiS56346.
    RefSeqiNP_418541.2. NC_000913.3.
    YP_492260.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77078; AAC77078; b4117.
    BAE78119; BAE78119; BAE78119.
    GeneIDi12934085.
    948638.
    KEGGiecj:Y75_p4004.
    eco:b4117.
    PATRICi32123799. VBIEscCol129921_4248.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93362 Genomic DNA. Translation: AAA23481.1 .
    U14003 Genomic DNA. Translation: AAA97017.1 . Different initiation.
    U00096 Genomic DNA. Translation: AAC77078.2 .
    AP009048 Genomic DNA. Translation: BAE78119.1 . Different initiation.
    M18425 Genomic DNA. No translation available.
    PIRi S56346.
    RefSeqi NP_418541.2. NC_000913.3.
    YP_492260.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VYC X-ray 2.40 A/B/C/D/E/F/G/H/I/J 1-755 [» ]
    ProteinModelPortali P28629.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-2903N.
    IntActi P28629. 6 interactions.
    MINTi MINT-1241522.
    STRINGi 511145.b4117.

    Proteomic databases

    PaxDbi P28629.
    PRIDEi P28629.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC77078 ; AAC77078 ; b4117 .
    BAE78119 ; BAE78119 ; BAE78119 .
    GeneIDi 12934085.
    948638.
    KEGGi ecj:Y75_p4004.
    eco:b4117.
    PATRICi 32123799. VBIEscCol129921_4248.

    Organism-specific databases

    EchoBASEi EB1464.
    EcoGenei EG11501. adiA.

    Phylogenomic databases

    eggNOGi COG1982.
    HOGENOMi HOG000164394.
    KOi K01584.
    OMAi ANDWVEC.
    OrthoDBi EOG696BRZ.
    PhylomeDBi P28629.

    Enzyme and pathway databases

    BioCyci EcoCyc:ARGDECARBOXDEG-MONOMER.
    ECOL316407:JW5731-MONOMER.
    MetaCyc:ARGDECARBOXDEG-MONOMER.
    BRENDAi 4.1.1.19. 2026.

    Miscellaneous databases

    EvolutionaryTracei P28629.
    PROi P28629.

    Gene expression databases

    Genevestigatori P28629.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.100.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProi IPR005308. OKR_de-COase_N.
    IPR011193. Orn/lys/arg_de-COase.
    IPR000310. Orn/Lys/Arg_deCO2ase_major_dom.
    IPR008286. Prn/Lys/Arg_de-COase_C.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view ]
    Pfami PF01276. OKR_DC_1. 1 hit.
    PF03711. OKR_DC_1_C. 1 hit.
    PF03709. OKR_DC_1_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF009393. Orn_decarb. 1 hit.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    SSF55904. SSF55904. 1 hit.
    PROSITEi PS00703. OKR_DC_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the adi gene, which encodes the biodegradative acid-induced arginine decarboxylase of Escherichia coli."
      Stim K.P., Bennett G.N.
      J. Bacteriol. 175:1221-1234(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
      Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
      Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "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.
    5. "Organisation of the regulatory region of the Escherichia coli melibiose operon."
      Webster C., Kempsell K., Booth I., Busby S.
      Gene 59:253-263(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-78.
    6. "Chemical properties of Escherichia coli lysine decarboxylase including a segment of its pyridoxal 5'-phosphate binding site."
      Sabo D.L., Fischer E.H.
      Biochemistry 13:670-676(1974) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-7.
      Strain: B.

    Entry informationi

    Entry nameiADIA_ECOLI
    AccessioniPrimary (citable) accession number: P28629
    Secondary accession number(s): P78138, Q2M6I7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 134 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3