SPEA_ECOLI
ID SPEA_ECOLI Reviewed; 658 AA.
AC P21170; Q2M9Q5;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Biosynthetic arginine decarboxylase;
DE Short=ADC;
DE EC=4.1.1.19 {ECO:0000269|PubMed:19603287, ECO:0000269|PubMed:2198270, ECO:0000269|PubMed:4571773};
GN Name=speA; OrderedLocusNames=b2938, JW2905;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, PROTEOLYTIC
RP PROCESSING, FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12;
RX PubMed=2198270; DOI=10.1128/jb.172.8.4631-4640.1990;
RA Moore R.C., Boyle S.M.;
RT "Nucleotide sequence and analysis of the speA gene encoding biosynthetic
RT arginine decarboxylase in Escherichia coli.";
RL J. Bacteriol. 172:4631-4640(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 635-658.
RC STRAIN=K12;
RX PubMed=1310091; DOI=10.1128/jb.174.3.758-764.1992;
RA Szumanski M.B.W., Boyle S.M.;
RT "Influence of cyclic AMP, agmatine, and a novel protein encoded by a
RT flanking gene on speB (agmatine ureohydrolase) in Escherichia coli.";
RL J. Bacteriol. 174:758-764(1992).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP ACTIVITY REGULATION, PATHWAY, AND SUBUNIT.
RC STRAIN=UW 44 / ATCC 27549;
RX PubMed=4571773; DOI=10.1016/s0021-9258(19)44245-2;
RA Wu W.H., Morris D.R.;
RT "Biosynthetic arginine decarboxylase from Escherichia coli. Purification
RT and properties.";
RL J. Biol. Chem. 248:1687-1695(1973).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19603287; DOI=10.1007/s11033-009-9617-0;
RA Song J., Zhou C., Liu R., Wu X., Wu D., Hu X., Ding Y.;
RT "Expression and purification of recombinant arginine decarboxylase (speA)
RT from Escherichia coli.";
RL Mol. Biol. Rep. 37:1823-1829(2010).
CC -!- FUNCTION: Catalyzes the biosynthesis of agmatine from arginine.
CC {ECO:0000269|PubMed:19603287, ECO:0000269|PubMed:2198270,
CC ECO:0000269|PubMed:4571773}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-arginine = agmatine + CO2; Xref=Rhea:RHEA:17641,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:58145; EC=4.1.1.19;
CC Evidence={ECO:0000269|PubMed:19603287, ECO:0000269|PubMed:2198270,
CC ECO:0000269|PubMed:4571773};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17642;
CC Evidence={ECO:0000269|PubMed:19603287, ECO:0000269|PubMed:2198270,
CC ECO:0000269|PubMed:4571773};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:4571773};
CC -!- ACTIVITY REGULATION: Down-regulated by polyamine end products
CC putrescine and spermidine. {ECO:0000269|PubMed:4571773}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.03 mM for L-arginine {ECO:0000269|PubMed:4571773};
CC pH dependence:
CC Optimum pH is 8.4. {ECO:0000269|PubMed:4571773};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius. Thermostable. Active from
CC 20 to 80 degrees Celsius. {ECO:0000269|PubMed:19603287};
CC -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC agmatine from L-arginine: step 1/1. {ECO:0000269|PubMed:4571773}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:4571773}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:2198270}.
CC -!- INDUCTION: By growth in an acidic enriched medium containing arginine
CC (biodegradative form), by growth in minimal media at neutral pH
CC (biosynthetic). Putrescine and spermidine repress the speA gene and
CC feedback inhibit ADC.
CC -!- PTM: Processed post-translationally to a 70 kDa mature form.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: ADC can be found in two forms: biodegradative and
CC biosynthetic. The biodegradative form may play a role in regulating pH
CC by consuming proteins.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC SpeA subfamily. {ECO:0000305}.
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DR EMBL; M31770; AAA24646.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69105.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75975.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77001.1; -; Genomic_DNA.
DR EMBL; M32363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A65079; A65079.
DR RefSeq; NP_417413.1; NC_000913.3.
DR RefSeq; WP_001300904.1; NZ_SSZK01000003.1.
DR PDB; 3NZQ; X-ray; 3.10 A; A/B=1-658.
DR PDBsum; 3NZQ; -.
DR AlphaFoldDB; P21170; -.
DR SMR; P21170; -.
DR BioGRID; 4262346; 13.
DR BioGRID; 851752; 4.
DR DIP; DIP-10905N; -.
DR IntAct; P21170; 16.
DR STRING; 511145.b2938; -.
DR jPOST; P21170; -.
DR PaxDb; P21170; -.
DR PRIDE; P21170; -.
DR DNASU; 947432; -.
DR EnsemblBacteria; AAC75975; AAC75975; b2938.
DR EnsemblBacteria; BAE77001; BAE77001; BAE77001.
DR GeneID; 947432; -.
DR KEGG; ecj:JW2905; -.
DR KEGG; eco:b2938; -.
DR PATRIC; fig|1411691.4.peg.3795; -.
DR EchoBASE; EB0952; -.
DR eggNOG; COG1166; Bacteria.
DR HOGENOM; CLU_027243_1_0_6; -.
DR InParanoid; P21170; -.
DR OMA; AVEYTQH; -.
DR PhylomeDB; P21170; -.
DR BioCyc; EcoCyc:ARGDECARBOXBIO-MON; -.
DR BioCyc; MetaCyc:ARGDECARBOXBIO-MON; -.
DR BRENDA; 4.1.1.19; 2026.
DR SABIO-RK; P21170; -.
DR UniPathway; UPA00186; UER00284.
DR EvolutionaryTrace; P21170; -.
DR PRO; PR:P21170; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0008792; F:arginine decarboxylase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR GO; GO:0006527; P:arginine catabolic process; IDA:EcoCyc.
DR GO; GO:0051289; P:protein homotetramerization; IDA:EcoCyc.
DR GO; GO:0009446; P:putrescine biosynthetic process; IDA:EcoCyc.
DR GO; GO:0033388; P:putrescine biosynthetic process from arginine; IMP:EcoCyc.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06830; PLPDE_III_ADC; 1.
DR Gene3D; 2.40.37.10; -; 1.
DR Gene3D; 3.20.20.10; -; 1.
DR HAMAP; MF_01417; SpeA; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR040634; Arg_decarb_HB.
DR InterPro; IPR041128; Arg_decarbox_C.
DR InterPro; IPR002985; Arg_decrbxlase.
DR InterPro; IPR022657; De-COase2_CS.
DR InterPro; IPR022644; De-COase2_N.
DR InterPro; IPR022653; De-COase2_pyr-phos_BS.
DR InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR InterPro; IPR029066; PLP-binding_barrel.
DR PANTHER; PTHR43295; PTHR43295; 1.
DR Pfam; PF17810; Arg_decarb_HB; 1.
DR Pfam; PF17944; Arg_decarbox_C; 1.
DR Pfam; PF02784; Orn_Arg_deC_N; 1.
DR PIRSF; PIRSF001336; Arg_decrbxlase; 1.
DR PRINTS; PR01180; ARGDCRBXLASE.
DR PRINTS; PR01179; ODADCRBXLASE.
DR SUPFAM; SSF50621; SSF50621; 1.
DR SUPFAM; SSF51419; SSF51419; 1.
DR TIGRFAMs; TIGR01273; speA; 1.
DR PROSITE; PS00878; ODR_DC_2_1; 1.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Lyase; Magnesium; Metal-binding; Periplasm;
KW Polyamine biosynthesis; Putrescine biosynthesis; Pyridoxal phosphate;
KW Reference proteome; Spermidine biosynthesis.
FT CHAIN 1..658
FT /note="Biosynthetic arginine decarboxylase"
FT /id="PRO_0000149960"
FT BINDING 307..317
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT MOD_RES 127
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 226
FT /note="A -> R (in Ref. 1; AAA24646)"
FT /evidence="ECO:0000305"
FT TURN 35..40
FT /evidence="ECO:0007829|PDB:3NZQ"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:3NZQ"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:3NZQ"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:3NZQ"
FT HELIX 93..114
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:3NZQ"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:3NZQ"
FT HELIX 132..139
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:3NZQ"
FT HELIX 152..162
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:3NZQ"
FT HELIX 177..188
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:3NZQ"
FT HELIX 200..212
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:3NZQ"
FT HELIX 247..259
FT /evidence="ECO:0007829|PDB:3NZQ"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:3NZQ"
FT HELIX 280..298
FT /evidence="ECO:0007829|PDB:3NZQ"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:3NZQ"
FT HELIX 332..350
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:3NZQ"
FT HELIX 362..366
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 369..380
FT /evidence="ECO:0007829|PDB:3NZQ"
FT HELIX 396..408
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 409..412
FT /evidence="ECO:0007829|PDB:3NZQ"
FT HELIX 417..436
FT /evidence="ECO:0007829|PDB:3NZQ"
FT HELIX 442..462
FT /evidence="ECO:0007829|PDB:3NZQ"
FT HELIX 468..470
FT /evidence="ECO:0007829|PDB:3NZQ"
FT HELIX 471..479
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 483..489
FT /evidence="ECO:0007829|PDB:3NZQ"
FT HELIX 491..494
FT /evidence="ECO:0007829|PDB:3NZQ"
FT HELIX 497..500
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 507..511
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 519..526
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 537..539
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 542..549
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 559..562
FT /evidence="ECO:0007829|PDB:3NZQ"
FT HELIX 570..572
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 583..589
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 595..601
FT /evidence="ECO:0007829|PDB:3NZQ"
FT HELIX 606..612
FT /evidence="ECO:0007829|PDB:3NZQ"
FT HELIX 617..627
FT /evidence="ECO:0007829|PDB:3NZQ"
FT HELIX 629..631
FT /evidence="ECO:0007829|PDB:3NZQ"
FT HELIX 635..649
FT /evidence="ECO:0007829|PDB:3NZQ"
FT STRAND 650..654
FT /evidence="ECO:0007829|PDB:3NZQ"
SQ SEQUENCE 658 AA; 73898 MW; 22613CEA5F957CC3 CRC64;
MSDDMSMGLP SSAGEHGVLR SMQEVAMSSQ EASKMLRTYN IAWWGNNYYD VNELGHISVC
PDPDVPEARV DLAQLVKTRE AQGQRLPALF CFPQILQHRL RSINAAFKRA RESYGYNGDY
FLVYPIKVNQ HRRVIESLIH SGEPLGLEAG SKAELMAVLA HAGMTRSVIV CNGYKDREYI
RLALIGEKMG HKVYLVIEKM SEIAIVLDEA ERLNVVPRLG VRARLASQGS GKWQSSGGEK
SKFGLAATQV LQLVETLREA GRLDSLQLLH FHLGSQMANI RDIATGVRES ARFYVELHKL
GVNIQCFDVG GGLGVDYEGT RSQSDCSVNY GLNEYANNII WAIGDACEEN GLPHPTVITE
SGRAVTAHHT VLVSNIIGVE RNEYTVPTAP AEDAPRALQS MWETWQEMHE PGTRRSLREW
LHDSQMDLHD IHIGYSSGIF SLQERAWAEQ LYLSMCHEVQ KQLDPQNRAH RPIIDELQER
MADKMYVNFS LFQSMPDAWG IDQLFPVLPL EGLDQVPERR AVLLDITCDS DGAIDHYIDG
DGIATTMPMP EYDPENPPML GFFMVGAYQE ILGNMHNLFG DTEAVDVFVF PDGSVEVELS
DEGDTVADML QYVQLDPKTL LTQFRDQVKK TDLDAELQQQ FLEEFEAGLY GYTYLEDE
