[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND PROTEOLYTIC PROCESSING. STRAIN=K12; PubMed=2198270 [NCBI, ExPASy, EBI, Israel, Japan] Moore R.C., Boyle S.M.; "Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli."; J. Bacteriol. 172:4631-4640(1990).
[2]	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).
[3]	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).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 635-658. STRAIN=K12; PubMed=1310091 [NCBI, ExPASy, EBI, Israel, Japan] Szumanski M.B.W., Boyle S.M.; "Influence of cyclic AMP, agmatine, and a novel protein encoded by a flanking gene on speB (agmatine ureohydrolase) in Escherichia coli."; J. Bacteriol. 174:758-764(1992).
[5]	CHARACTERIZATION. STRAIN=UW 44 / ATCC 27549; PubMed=4571773 [NCBI, ExPASy, EBI, Israel, Japan] Wu W.H., Morris D.R.; "Biosynthetic arginine decarboxylase from Escherichia coli. Purification and properties."; J. Biol. Chem. 248:1687-1695(1973).

Comments

FUNCTION: Catalyzes the biosynthesis of agmatine from arginine (By similarity).
CATALYTIC ACTIVITY: L-arginine = agmatine + CO₂.
COFACTOR: Pyridoxal phosphate.
COFACTOR: Magnesium.
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 8.4;
PATHWAY: Amino-acid degradation; L-arginine degradation via ADC pathway; agmatine from L-arginine: step 1/1 .
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Periplasm.
INDUCTION: By growth in an acidic enriched medium containing arginine (biodegradative form), by growth in minimal media at neutral pH (biosynthetic). Putrescine and spermidine repress the speA gene and feedback inhibit ADC.
PTM: Processed post-translationally to a 70 kDa mature form.
PTM: The N-terminus is blocked.
MISCELLANEOUS: ADC can be found in two forms: biodegradative and biosynthetic. The biodegradative form may play a role in regulating pH by consuming proteins.
SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily.

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

M31770; AAA24646.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U28377; AAA69105.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75975.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77001.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M32363; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]

PIR

A65079; A65079.

RefSeq

AP_003495.1; -.
NP_417413.1; -.

3D structure databases

ModBase

P21170.

Protein-protein interaction databases

DIP

DIP:307N; -.

Enzyme and pathway databases

BioCyc

EcoCyc:ARGDECARBOXBIO-MON; -.
MetaCyc:ARGDECARBOXBIO-MON; -.

Organism-specific databases

EchoBASE

EB0952; -.

EcoGene

EG10959; speA.

Ontologies

GO:0042597;	Cellular component: periplasmic space (inferred from electronic annotation from UniProtKB-KW).
GO:0008792;	Molecular function: arginine decarboxylase activity (inferred from electronic annotation from HAMAP).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006527;	Biological process: arginine catabolic process (inferred from electronic annotation from InterPro).
GO:0009446;	Biological process: putrescine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0008295;	Biological process: spermidine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01417; -; 1.
PBIL [Tree]

InterPro

IPR002985; Arg_decrbxlase.
IPR000183; De-COase2.
Graphical view of domain structure.

PANTHER

PTHR11482:SF3; Arg_decrbxlase; 1.

Pfam

PF02784; Orn_Arg_deC_N; 1.
PF00278; Orn_DAP_Arg_deC; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001336; Arg_decrbxlase; 1.

PRINTS

PR01180; ARGDCRBXLASE.
PR01179; ODADCRBXLASE.

TIGRFAMs

TIGR01273; speA; 1.

PROSITE

PS00878; ODR_DC_2_1; 1.
PS00879; ODR_DC_2_2; 1.

ProtoNet

P21170.

Genome annotation databases

GeneID

947432; -.

GenomeReviews

U00096_GR; b2938.
AP009048_GR; JW2905.

KEGG

ecj:JW2905; -.
eco:b2938; -.

Phylogenomic databases

HOGENOM

P21170; -.

Genome annotation databases

CMR

P21170; b2938.

Other

UniRef

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

Keywords

Complete proteome; Decarboxylase; Lyase; Magnesium; Metal-binding; Periplasm; Polyamine biosynthesis; Putrescine biosynthesis; Pyridoxal phosphate; Spermidine biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 658`	`658`	`Biosynthetic arginine decarboxylase.`	`PRO_0000149960`
`REGION`	`307 317`	`11`	`Substrate-binding (Potential).`
`BINDING`	`127 127`		`Pyridoxal phosphate (covalent) (By similarity).`
`CONFLICT`	`226 226`		`A -> R (in Ref. 1; AAA24646).`

Sequence information

Length: 658 AA [This is the length of the unprocessed precursor]

Molecular weight: 73898 Da [This is the MW of the unprocessed precursor]

CRC64: 22613CEA5F957CC3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSDDMSMGLP SSAGEHGVLR SMQEVAMSSQ EASKMLRTYN IAWWGNNYYD VNELGHISVC 

        70         80         90        100        110        120 
PDPDVPEARV DLAQLVKTRE AQGQRLPALF CFPQILQHRL RSINAAFKRA RESYGYNGDY 

       130        140        150        160        170        180 
FLVYPIKVNQ HRRVIESLIH SGEPLGLEAG SKAELMAVLA HAGMTRSVIV CNGYKDREYI 

       190        200        210        220        230        240 
RLALIGEKMG HKVYLVIEKM SEIAIVLDEA ERLNVVPRLG VRARLASQGS GKWQSSGGEK 

       250        260        270        280        290        300 
SKFGLAATQV LQLVETLREA GRLDSLQLLH FHLGSQMANI RDIATGVRES ARFYVELHKL 

       310        320        330        340        350        360 
GVNIQCFDVG GGLGVDYEGT RSQSDCSVNY GLNEYANNII WAIGDACEEN GLPHPTVITE 

       370        380        390        400        410        420 
SGRAVTAHHT VLVSNIIGVE RNEYTVPTAP AEDAPRALQS MWETWQEMHE PGTRRSLREW 

       430        440        450        460        470        480 
LHDSQMDLHD IHIGYSSGIF SLQERAWAEQ LYLSMCHEVQ KQLDPQNRAH RPIIDELQER 

       490        500        510        520        530        540 
MADKMYVNFS LFQSMPDAWG IDQLFPVLPL EGLDQVPERR AVLLDITCDS DGAIDHYIDG 

       550        560        570        580        590        600 
DGIATTMPMP EYDPENPPML GFFMVGAYQE ILGNMHNLFG DTEAVDVFVF PDGSVEVELS 

       610        620        630        640        650 
DEGDTVADML QYVQLDPKTL LTQFRDQVKK TDLDAELQQQ FLEEFEAGLY GYTYLEDE

P21170 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