ID   ADIA_ECOLI              Reviewed;         755 AA.
AC   P28629; P78138; Q2M6I7;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   16-DEC-2008, entry version 86.
DE   RecName: Full=Biodegradative arginine decarboxylase;
DE            Short=ADC;
DE            EC=4.1.1.19;
GN   Name=adiA; Synonyms=adi; OrderedLocusNames=b4117, JW5731;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   MEDLINE=93186686; PubMed=8383109;
RA   Stim K.P., Bennett G.N.;
RT   "Nucleotide sequence of the adi gene, which encodes the biodegradative
RT   acid-induced arginine decarboxylase of Escherichia coli.";
RL   J. Bacteriol. 175:1221-1234(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=95334362; PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.,
RA   Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the
RT   region from 92.8 through 100 minutes.";
RL   Nucleic Acids Res. 23:2105-2119(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; 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.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [4]
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
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-78.
RX   MEDLINE=88137961; PubMed=2830169; DOI=10.1016/0378-1119(87)90333-7;
RA   Webster C., Kempsell K., Booth I., Busby S.;
RT   "Organisation of the regulatory region of the Escherichia coli
RT   melibiose operon.";
RL   Gene 59:253-263(1987).
RN   [6]
RP   PROTEIN SEQUENCE OF 1-7.
RX   MEDLINE=74086944; PubMed=4204273; DOI=10.1021/bi00701a006;
RA   Sabo D.L., Fischer E.H.;
RT   "Chemical properties of Escherichia coli lysine decarboxylase
RT   including a segment of its pyridoxal 5'-phosphate binding site.";
RL   Biochemistry 13:670-676(1974).
CC   -!- FUNCTION: ADC can be found in two forms: biodegradative and
CC       biosynthetic. The biodegradative form may play a role in
CC       regulating pH by consuming proteins.
CC   -!- CATALYTIC ACTIVITY: L-arginine = agmatine + CO(2).
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- SUBUNIT: Homodecamer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: Under conditions of acidic pH, anaerobiosis and rich
CC       medium.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I
CC       family.
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DR   EMBL; M93362; AAA23481.1; -; Genomic_DNA.
DR   EMBL; U14003; AAA97017.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC77078.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP009048; BAE78119.1; ALT_INIT; Genomic_DNA.
DR   EMBL; M18425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; S56346; S56346.
DR   RefSeq; AP_004618.1; -.
DR   RefSeq; NP_418541.1; -.
DR   HSSP; P43099; 1C4K.
DR   DIP; DIP:2903N; -.
DR   GeneID; 948638; -.
DR   GenomeReviews; AP009048_GR; JW5731.
DR   GenomeReviews; U00096_GR; b4117.
DR   KEGG; ecj:JW5731; -.
DR   KEGG; eco:b4117; -.
DR   EchoBASE; EB1464; -.
DR   EcoGene; EG11501; adiA.
DR   HOGENOM; P28629; -.
DR   BioCyc; EcoCyc:ARGDECARBOXDEG-MON; -.
DR   BioCyc; MetaCyc:ARGDECARBOXDEG-MON; -.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   InterPro; IPR000310; Decarbxylse1.
DR   InterPro; IPR005308; OKR_de-COase_N.
DR   InterPro; IPR011193; Orn/lys/arg_de-COase.
DR   InterPro; IPR008286; Prn/Lys/Arg_de-COase_C.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Gene3D; G3DSA:3.90.100.10; Decarbxylse_C; 1.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1.
DR   Pfam; PF01276; OKR_DC_1; 1.
DR   Pfam; PF03711; OKR_DC_1_C; 1.
DR   Pfam; PF03709; OKR_DC_1_N; 1.
DR   PIRSF; PIRSF009393; Orn_decarb; 1.
DR   PROSITE; PS00703; OKR_DC_1; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Decarboxylase;
KW   Direct protein sequencing; Lyase; Pyridoxal phosphate.
FT   CHAIN         1    755       Biodegradative arginine decarboxylase.
FT                                /FTId=PRO_0000201149.
FT   BINDING     386    386       Pyridoxal phosphate (covalent).
FT   CONFLICT     75     75       L -> P (in Ref. 5).
SQ   SEQUENCE   755 AA;  84425 MW;  0FCB715144649F8F CRC64;
     MKVLIVESEF LHQDTWVGNA VERLADALSQ QNVTVIKSTS FDDGFAILSS NEAIDCLMFS
     YQMEHPDEHQ NVRQLIGKLH ERQQNVPVFL LGDREKALAA MDRDLLELVD EFAWILEDTA
     DFIAGRAVAA MTRYRQQLLP PLFSALMKYS DIHEYSWAAP GHQGGVGFTK TPAGRFYHDY
     YGENLFRTDM GIERTSLGSL LDHTGAFGES EKYAARVFGA DRSWSVVVGT SGSNRTIMQA
     CMTDNDVVVV DRNCHKSIEQ GLMLTGAKPV YMVPSRNRYG IIGPIYPQEM QPETLQKKIS
     ESPLTKDKAG QKPSYCVVTN CTYDGVCYNA KEAQDLLEKT SDRLHFDEAW YGYARFNPIY
     ADHYAMRGEP GDHNGPTVFA THSTHKLLNA LSQASYIHVR EGRGAINFSR FNQAYMMHAT
     TSPLYAICAS NDVAVSMMDG NSGLSLTQEV IDEAVDFRQA MARLYKEFTA DGSWFFKPWN
     KEVVTDPQTG KTYDFADAPT KLLTTVQDCW VMHPGESWHG FKDIPDNWSM LDPIKVSILA
     PGMGEDGELE ETGVPAALVT AWLGRHGIVP TRTTDFQIMF LFSMGVTRGK WGTLVNTLCS
     FKRHYDANTP LAQVMPELVE QYPDTYANMG IHDLGDTMFA WLKENNPGAR LNEAYSGLPV
     AEVTPREAYN AIVDNNVELV SIENLPGRIA ANSVIPYPPG IPMLLSGENF GDKNSPQVSY
     LRSLQSWDHH FPGFEHETEG TEIIDGIYHV MCVKA
//