[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; PubMed=8383109 [NCBI, ExPASy, EBI, Israel, Japan] Stim K.P., Bennett G.N.; "Nucleotide sequence of the adi gene, which encodes the biodegradative acid-induced arginine decarboxylase of Escherichia coli."; J. Bacteriol. 175:1221-1234(1993).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1093/nar/23.12.2105; PubMed=7610040 [NCBI, ExPASy, EBI, Israel, Japan] Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.; "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."; Nucleic Acids Res. 23:2105-2119(1995).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-78. DOI=10.1016/0378-1119(87)90333-7; PubMed=2830169 [NCBI, ExPASy, EBI, Israel, Japan] Webster C., Kempsell K., Booth I., Busby S.; "Organisation of the regulatory region of the Escherichia coli melibiose operon."; Gene 59:253-263(1987).
[6]	PROTEIN SEQUENCE OF 1-7. DOI=10.1021/bi00701a006; PubMed=4204273 [NCBI, ExPASy, EBI, Israel, Japan] Sabo D.L., Fischer E.H.; "Chemical properties of Escherichia coli lysine decarboxylase including a segment of its pyridoxal 5'-phosphate binding site."; Biochemistry 13:670-676(1974).

Comments

FUNCTION: ADC can be found in two forms: biodegradative and biosynthetic. The biodegradative form may play a role in regulating pH by consuming proteins.
CATALYTIC ACTIVITY: L-arginine = agmatine + CO₂.
COFACTOR: Pyridoxal phosphate.
SUBUNIT: Homodecamer.
SUBCELLULAR LOCATION: Cytoplasm.
INDUCTION: Under conditions of acidic pH, anaerobiosis and rich medium.
SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M93362; AAA23481.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U14003; AAA97017.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC77078.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE78119.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M18425; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]

PIR

S56346; S56346.

RefSeq

AP_004618.1; -.
NP_418541.1; -.

3D structure databases

HSSP

P43099; 1C4K. [HSSP ENTRY / PDB]

ModBase

P28629.

Protein-protein interaction databases

DIP

DIP:2903N; -.

Enzyme and pathway databases

BioCyc

EcoCyc:ARGDECARBOXDEG-MON; -.
MetaCyc:ARGDECARBOXDEG-MON; -.

Organism-specific databases

EchoBASE

EB1464; -.

EcoGene

EG11501; adiA.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from direct assay from UniProtKB).
GO:0008792;	Molecular function: arginine decarboxylase activity (inferred from electronic annotation from EC).
GO:0030170;	Molecular function: pyridoxal phosphate binding (inferred from electronic annotation from InterPro).
GO:0006520;	Biological process: amino acid metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000310; Decarbxylse1.
IPR005308; OKR_de-COase_N.
IPR011193; Orn/lys/arg_de-COase.
IPR008286; Prn/Lys/Arg_de-COase_C.
IPR015421; PyrdxlP-dep_Trfase_major_sub1.
IPR015422; PyrdxlP-dep_Trfase_major_sub2.
Graphical view of domain structure.

Gene3D

G3DSA:3.90.100.10; Decarbxylse_C; 1.
G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1.

Pfam

PF01276; OKR_DC_1; 1.
PF03711; OKR_DC_1_C; 1.
PF03709; OKR_DC_1_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF009393; Orn_decarb; 1.

PROSITE

PS00703; OKR_DC_1; 1.

Genome annotation databases

GeneID

948638; -.

GenomeReviews

U00096_GR; b4117.
AP009048_GR; JW5731.

KEGG

ecj:JW5731; -.
eco:b4117; -.

Phylogenomic databases

HOGENOM

P28629; -.

Genome annotation databases

CMR

P28629; b4117.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Decarboxylase; Direct protein sequencing; Lyase; Pyridoxal phosphate.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 755`	`755`	`Biodegradative arginine decarboxylase.`	`PRO_0000201149`
`BINDING`	`386 386`		`Pyridoxal phosphate (covalent).`
`CONFLICT`	`75 75`		`L -> P (in Ref. 5).`

Sequence information

Length: 755 AA [This is the length of the unprocessed precursor]

Molecular weight: 84425 Da [This is the MW of the unprocessed precursor]

CRC64: 0FCB715144649F8F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKVLIVESEF LHQDTWVGNA VERLADALSQ QNVTVIKSTS FDDGFAILSS NEAIDCLMFS 

        70         80         90        100        110        120 
YQMEHPDEHQ NVRQLIGKLH ERQQNVPVFL LGDREKALAA MDRDLLELVD EFAWILEDTA 

       130        140        150        160        170        180 
DFIAGRAVAA MTRYRQQLLP PLFSALMKYS DIHEYSWAAP GHQGGVGFTK TPAGRFYHDY 

       190        200        210        220        230        240 
YGENLFRTDM GIERTSLGSL LDHTGAFGES EKYAARVFGA DRSWSVVVGT SGSNRTIMQA 

       250        260        270        280        290        300 
CMTDNDVVVV DRNCHKSIEQ GLMLTGAKPV YMVPSRNRYG IIGPIYPQEM QPETLQKKIS 

       310        320        330        340        350        360 
ESPLTKDKAG QKPSYCVVTN CTYDGVCYNA KEAQDLLEKT SDRLHFDEAW YGYARFNPIY 

       370        380        390        400        410        420 
ADHYAMRGEP GDHNGPTVFA THSTHKLLNA LSQASYIHVR EGRGAINFSR FNQAYMMHAT 

       430        440        450        460        470        480 
TSPLYAICAS NDVAVSMMDG NSGLSLTQEV IDEAVDFRQA MARLYKEFTA DGSWFFKPWN 

       490        500        510        520        530        540 
KEVVTDPQTG KTYDFADAPT KLLTTVQDCW VMHPGESWHG FKDIPDNWSM LDPIKVSILA 

       550        560        570        580        590        600 
PGMGEDGELE ETGVPAALVT AWLGRHGIVP TRTTDFQIMF LFSMGVTRGK WGTLVNTLCS 

       610        620        630        640        650        660 
FKRHYDANTP LAQVMPELVE QYPDTYANMG IHDLGDTMFA WLKENNPGAR LNEAYSGLPV 

       670        680        690        700        710        720 
AEVTPREAYN AIVDNNVELV SIENLPGRIA ANSVIPYPPG IPMLLSGENF GDKNSPQVSY 

       730        740        750 
LRSLQSWDHH FPGFEHETEG TEIIDGIYHV MCVKA

P28629 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools