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Database: UniProt/TrEMBL
Entry: A1AFC7_ECOK1
LinkDB: A1AFC7_ECOK1
Original site: A1AFC7_ECOK1 
ID   A1AFC7_ECOK1            Unreviewed;       658 AA.
AC   A1AFC7;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   26-NOV-2014, entry version 52.
DE   RecName: Full=Biosynthetic arginine decarboxylase {ECO:0000256|HAMAP-Rule:MF_01417};
DE            Short=ADC {ECO:0000256|HAMAP-Rule:MF_01417};
DE            EC=4.1.1.19 {ECO:0000256|HAMAP-Rule:MF_01417};
GN   Name=speA {ECO:0000256|HAMAP-Rule:MF_01417,
GN   ECO:0000313|EMBL:ABJ02367.1};
GN   ORFNames=APECO1_3590 {ECO:0000313|EMBL:ABJ02367.1};
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955 {ECO:0000313|EMBL:ABJ02367.1, ECO:0000313|Proteomes:UP000008216};
RN   [1] {ECO:0000313|EMBL:ABJ02367.1, ECO:0000313|Proteomes:UP000008216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APEC O1 {ECO:0000313|EMBL:ABJ02367.1};
RX   PubMed=17293413; DOI=10.1128/JB.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P.,
RA   Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R.,
RA   Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain
RT   O1:K1:H7 shares strong similarities with human extraintestinal
RT   pathogenic E. coli genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
CC   -!- FUNCTION: Catalyzes the biosynthesis of agmatine from arginine.
CC       {ECO:0000256|HAMAP-Rule:MF_01417, ECO:0000256|SAAS:SAAS00007915}.
CC   -!- CATALYTIC ACTIVITY: L-arginine = agmatine + CO(2).
CC       {ECO:0000256|HAMAP-Rule:MF_01417, ECO:0000256|RuleBase:RU003740,
CC       ECO:0000256|SAAS:SAAS00098902}.
CC   -!- COFACTOR:
CC       Note=Magnesium. {ECO:0000256|HAMAP-Rule:MF_01417,
CC       ECO:0000256|RuleBase:RU003740, ECO:0000256|SAAS:SAAS00098917};
CC   -!- COFACTOR:
CC       Note=Pyridoxal phosphate. {ECO:0000256|HAMAP-Rule:MF_01417,
CC       ECO:0000256|SAAS:SAAS00098939};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC       agmatine from L-arginine: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01417}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II
CC       family. SpeA subfamily. {ECO:0000256|HAMAP-Rule:MF_01417}.
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DR   EMBL; CP000468; ABJ02367.1; -; Genomic_DNA.
DR   RefSeq; YP_854156.1; NC_008563.1.
DR   ProteinModelPortal; A1AFC7; -.
DR   STRING; 405955.APECO1_3590; -.
DR   EnsemblBacteria; ABJ02367; ABJ02367; APECO1_3590.
DR   GeneID; 4493225; -.
DR   KEGG; ecv:APECO1_3590; -.
DR   PATRIC; 18218051; VBIEscCol127180_3265.
DR   eggNOG; COG1166; -.
DR   HOGENOM; HOG000029191; -.
DR   KO; K01585; -.
DR   OMA; IDHYVDG; -.
DR   OrthoDB; EOG676Z0R; -.
DR   UniPathway; UPA00186; UER00284.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR   GO; GO:0009446; P:putrescine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 2.40.37.10; -; 2.
DR   Gene3D; 3.20.20.10; -; 1.
DR   HAMAP; MF_01417; SpeA; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR002985; Arg_decrbxlase.
DR   InterPro; IPR022643; De-COase2_C.
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   Pfam; PF02784; Orn_Arg_deC_N; 1.
DR   Pfam; PF00278; Orn_DAP_Arg_deC; 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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008216};
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_01417,
KW   ECO:0000256|RuleBase:RU003740};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01417,
KW   ECO:0000256|RuleBase:RU003740};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01417,
KW   ECO:0000256|SAAS:SAAS00098959};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01417,
KW   ECO:0000256|SAAS:SAAS00007726};
KW   Polyamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01417,
KW   ECO:0000256|SAAS:SAAS00007823};
KW   Putrescine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01417};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01417,
KW   ECO:0000256|SAAS:SAAS00099000};
KW   Spermidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01417,
KW   ECO:0000256|RuleBase:RU003740}.
FT   REGION      307    317       Substrate-binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01417}.
FT   MOD_RES     127    127       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01417}.
SQ   SEQUENCE   658 AA;  73886 MW;  87106BF8727B6EE2 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 IHIGYSSGTF SLQERAWAEQ LYLSMCHEVQ KQLDPQNRAH RPIIDELQER
     MADKMYVNFS LFQSMPDAWG IDQLFPVLPL EGLDQVPERR AVLLDITCDS DGAIDHYIDG
     DGIATTMPMP EYDPENPPML GFFMVGAYQE ILGNMHNLFG DTEAVDVFVF PDGSVEVELS
     DEGDTVADML QYVQLDPKTL LTQFRDQVKK TDLDAELQQQ FLEEFEAGLY GYTYLEDE
//
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