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P21885

- SPEA_BACSU

UniProt

P21885 - SPEA_BACSU

Protein

Arginine decarboxylase

Gene

speA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (01 Dec 1992)
      Previous versions | rss
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    Functioni

    Catalyzes the formation of agmatine from arginine.

    Catalytic activityi

    L-arginine = agmatine + CO2.

    Cofactori

    Pyridoxal phosphate.

    Pathwayi

    GO - Molecular functioni

    1. arginine decarboxylase activity Source: UniProtKB-EC
    2. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. putrescine biosynthetic process Source: UniProtKB-KW
    2. spermidine biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

    Polyamine biosynthesis, Putrescine biosynthesis, Spermidine biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciBSUB:BSU14630-MONOMER.
    UniPathwayiUPA00186; UER00284.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arginine decarboxylase (EC:4.1.1.19)
    Gene namesi
    Name:speA
    Synonyms:cad
    Ordered Locus Names:BSU14630
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU14630. [Micado]

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 490490Arginine decarboxylasePRO_0000201147Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei226 – 2261N6-(pyridoxal phosphate)lysineBy similarity

    Proteomic databases

    PaxDbiP21885.

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU14630.

    Structurei

    3D structure databases

    ProteinModelPortaliP21885.
    SMRiP21885. Positions 1-480.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1982.
    HOGENOMiHOG000083489.
    KOiK01585.
    OMAiHIQMELS.
    OrthoDBiEOG61CKX5.
    PhylomeDBiP21885.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.100.10. 1 hit.
    InterProiIPR000310. Orn/Lys/Arg_deCO2ase_major_dom.
    IPR008286. Prn/Lys/Arg_de-COase_C.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    [Graphical view]
    PfamiPF01276. OKR_DC_1. 1 hit.
    PF03711. OKR_DC_1_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 1 hit.
    SSF55904. SSF55904. 1 hit.
    PROSITEiPS00703. OKR_DC_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P21885-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQHETPLYT GLKKHASRQP VQFHIPGHKK GAGMDPEFRQ FIGENALSID    50
    LINIEPLDDL HAPKGIIKQA QDLAAEAFGA DHTFFSVQGT SGAIMTMVMA 100
    VCGPGDKIII PRNVHKSIMT AIVFSGAVPI FIHPEIDNEL GISHGITLES 150
    AKRALTEHPD AKGLLVINPT YFGVAADLKS IVELAHSFDV PVLVDEAHGV 200
    HIHFHDELPL SAMQAGADIA ATSVHKLGGS LTQSSILNMR EGLVSKDRVQ 250
    SILSMLTTTS TSYLLLASLD VARKRLATEG RQLAEETLKL ANQTRDRLNQ 300
    IEGIYCVGSE ILGSKAAYSY DPTKLIISVK SLGLTGHDVE KWLRESFNIE 350
    VELSDLYNIL CIFTPGDSQN DADRLVEALT EIAQQMSEQD VTHQQTEVLL 400
    PEIPLLAMTP RDAFYANTEV IPLKEASGRI IAEFVMVYPP GIPIFIPGEI 450
    ITEENISYIF KNLDAGLPVQ GPEDSTLHMI RVIKEQKAIQ 490
    Length:490
    Mass (Da):53,583
    Last modified:December 1, 1992 - v2
    Checksum:i1AC7ACAE24F4F6D2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58433 Genomic DNA. Translation: CAA41337.1.
    AF012285 Genomic DNA. Translation: AAC24937.1.
    AL009126 Genomic DNA. Translation: CAB13336.1.
    M57435 Genomic DNA. Translation: AAA62686.1.
    PIRiA54546.
    RefSeqiNP_389346.1. NC_000964.3.
    WP_003244780.1. NZ_CM000487.1.

    Genome annotation databases

    EnsemblBacteriaiCAB13336; CAB13336; BSU14630.
    GeneIDi936002.
    KEGGibsu:BSU14630.
    PATRICi18974721. VBIBacSub10457_1552.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58433 Genomic DNA. Translation: CAA41337.1 .
    AF012285 Genomic DNA. Translation: AAC24937.1 .
    AL009126 Genomic DNA. Translation: CAB13336.1 .
    M57435 Genomic DNA. Translation: AAA62686.1 .
    PIRi A54546.
    RefSeqi NP_389346.1. NC_000964.3.
    WP_003244780.1. NZ_CM000487.1.

    3D structure databases

    ProteinModelPortali P21885.
    SMRi P21885. Positions 1-480.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU14630.

    Proteomic databases

    PaxDbi P21885.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13336 ; CAB13336 ; BSU14630 .
    GeneIDi 936002.
    KEGGi bsu:BSU14630.
    PATRICi 18974721. VBIBacSub10457_1552.

    Organism-specific databases

    GenoListi BSU14630. [Micado ]

    Phylogenomic databases

    eggNOGi COG1982.
    HOGENOMi HOG000083489.
    KOi K01585.
    OMAi HIQMELS.
    OrthoDBi EOG61CKX5.
    PhylomeDBi P21885.

    Enzyme and pathway databases

    UniPathwayi UPA00186 ; UER00284 .
    BioCyci BSUB:BSU14630-MONOMER.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.100.10. 1 hit.
    InterProi IPR000310. Orn/Lys/Arg_deCO2ase_major_dom.
    IPR008286. Prn/Lys/Arg_de-COase_C.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    [Graphical view ]
    Pfami PF01276. OKR_DC_1. 1 hit.
    PF03711. OKR_DC_1_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53383. SSF53383. 1 hit.
    SSF55904. SSF55904. 1 hit.
    PROSITEi PS00703. OKR_DC_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing the lysine decarboxylase of Bacillus subtilis."
      Hemilae H., Koivula T., Paulin L.
      Submitted (MAR-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "The ampS-nprE (124 degrees-127 degrees) region of the Bacillus subtilis 168 chromosome: sequencing of a 27 kb segment and identification of several genes in the area."
      Winters P., Caldwell R.M., Enfield L., Ferrari E.
      Microbiology 142:3033-3037(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    4. "Secretory S complex of Bacillus subtilis: sequence analysis and identity to pyruvate dehydrogenase."
      Hemilae H.O., Palva A., Paulin L., Arvidson S., Palva I.
      J. Bacteriol. 172:5052-5063(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-490.
      Strain: 168.
    5. "Sequence of a PAL-related lipoprotein from Bacillus subtilis."
      Hemilae H.O.
      FEMS Microbiol. Lett. 66:37-41(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 485-490.
    6. "Characterization of polyamine synthesis pathway in Bacillus subtilis 168."
      Sekowska A., Bertin P., Danchin A.
      Mol. Microbiol. 29:851-858(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF POLYAMINE PATHWAY.

    Entry informationi

    Entry nameiSPEA_BACSU
    AccessioniPrimary (citable) accession number: P21885
    Secondary accession number(s): P26934
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 115 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally (PubMed:8969500) thought to be a lysine decarboxylase and was consequently named cad.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3