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P21885

- SPEA_BACSU

UniProt

P21885 - SPEA_BACSU

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Protein

Arginine decarboxylase

Gene

speA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the formation of agmatine from arginine.

Catalytic activityi

L-arginine = agmatine + CO2.

Cofactori

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
Complete GO annotation...

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-KW
Complete GO annotation...

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.
InParanoidiP21885.
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

        10         20         30         40         50
MSQHETPLYT GLKKHASRQP VQFHIPGHKK GAGMDPEFRQ FIGENALSID
60 70 80 90 100
LINIEPLDDL HAPKGIIKQA QDLAAEAFGA DHTFFSVQGT SGAIMTMVMA
110 120 130 140 150
VCGPGDKIII PRNVHKSIMT AIVFSGAVPI FIHPEIDNEL GISHGITLES
160 170 180 190 200
AKRALTEHPD AKGLLVINPT YFGVAADLKS IVELAHSFDV PVLVDEAHGV
210 220 230 240 250
HIHFHDELPL SAMQAGADIA ATSVHKLGGS LTQSSILNMR EGLVSKDRVQ
260 270 280 290 300
SILSMLTTTS TSYLLLASLD VARKRLATEG RQLAEETLKL ANQTRDRLNQ
310 320 330 340 350
IEGIYCVGSE ILGSKAAYSY DPTKLIISVK SLGLTGHDVE KWLRESFNIE
360 370 380 390 400
VELSDLYNIL CIFTPGDSQN DADRLVEALT EIAQQMSEQD VTHQQTEVLL
410 420 430 440 450
PEIPLLAMTP RDAFYANTEV IPLKEASGRI IAEFVMVYPP GIPIFIPGEI
460 470 480 490
ITEENISYIF KNLDAGLPVQ GPEDSTLHMI RVIKEQKAIQ
Length:490
Mass (Da):53,583
Last modified:December 1, 1992 - v2
Checksum:i1AC7ACAE24F4F6D2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
InParanoidi P21885.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 117 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