Reviewed, UniProtKB/Swiss-Prot P21170 (SPEA_ECOLI)

Names and origin

Protein names

Recommended name:
    Biosynthetic arginine decarboxylase
      Short name=ADC
    EC=4.1.1.19

Gene names

Name:	speA
Ordered Locus Names:	b2938, JW2905

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	658 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the biosynthesis of agmatine from arginine By similarity.
Catalytic activity	L-arginine = agmatine + CO(2).
Cofactor	Pyridoxal phosphate. Magnesium.
Pathway	Amino-acid degradation; L-arginine degradation via ADC pathway; agmatine from L-arginine: step 1/1.
Subunit structure	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.
Post-translational modification	Processed post-translationally to a 70 kDa mature form. 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.
Sequence similarities	Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily.
Biophysicochemical properties	pH dependence: Optimum pH is 8.4.

Ontologies

Keywords
Biological process	Polyamine biosynthesis Putrescine biosynthesis Spermidine biosynthesis
Cellular component	Periplasm
Ligand	Magnesium Metal-binding Pyridoxal phosphate
Molecular function	Decarboxylase Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	spermidine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	arginine decarboxylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 658	658	Biosynthetic arginine decarboxylase
Regions
	Region	307 – 317	11	Substrate-binding Potential
Sites
	Binding site	127	1	Pyridoxal phosphate (covalent) By similarity
Experimental info
	Sequence conflict	226	1	A → R in AAA24646. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P21170-1 [UniParc]. Last modified August 29, 2003. Version 2. Checksum: 22613CEA5F957CC3	FASTA	658	73,898
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli." Moore R.C., Boyle S.M. J. Bacteriol. 172:4631-4640(1990) [PubMed: 2198270] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING. Strain: K12.
[2]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Influence of cyclic AMP, agmatine, and a novel protein encoded by a flanking gene on speB (agmatine ureohydrolase) in Escherichia coli." Szumanski M.B.W., Boyle S.M. J. Bacteriol. 174:758-764(1992) [PubMed: 1310091] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 635-658. Strain: K12.
[5]	"Biosynthetic arginine decarboxylase from Escherichia coli. Purification and properties." Wu W.H., Morris D.R. J. Biol. Chem. 248:1687-1695(1973) [PubMed: 4571773] [Abstract] Cited for: CHARACTERIZATION. Strain: UW 44 / ATCC 27549.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M31770 Genomic DNA. Translation: AAA24646.1. U28377 Genomic DNA. Translation: AAA69105.1. U00096 Genomic DNA. Translation: AAC75975.1. AP009048 Genomic DNA. Translation: BAE77001.1. M32363 Genomic DNA. No translation available.
PIR	A65079.
RefSeq	AP_003495.1. NP_417413.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:307N.
IntAct	P21170.
Genome annotation databases
GeneID	947432.
GenomeReviews	Gene locus b2938 in contig U00096_GR. Gene locus JW2905 in contig AP009048_GR.
KEGG	ecj:JW2905. eco:b2938.
Organism-specific databases
EchoBASE	EB0952.
EcoGene	EG10959. speA.
CMR	Search...
Phylogenomic databases
HOGENOM	P21170.
Enzyme and pathway databases
BioCyc	EcoCyc:ARGDECARBOXBIO-MON. MetaCyc:ARGDECARBOXBIO-MON.
Family and domain databases
HAMAP	MF_01417. [Tree]
InterPro	IPR002985. Arg_decrbxlase. IPR000183. De-COase2. [Graphical view]
PANTHER	PTHR11482:SF3. Arg_decrbxlase. 1 hit.
Pfam	PF02784. Orn_Arg_deC_N. 1 hit. PF00278. Orn_DAP_Arg_deC. 1 hit. [Graphical view]
PIRSF	PIRSF001336. Arg_decrbxlase. 1 hit.
PRINTS	PR01180. ARGDCRBXLASE. PR01179. ODADCRBXLASE.
TIGRFAMs	TIGR01273. speA. 1 hit.
PROSITE	PS00878. ODR_DC_2_1. 1 hit. PS00879. ODR_DC_2_2. 1 hit. [Graphical view]
ProDom	P21170. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

SPEA_ECOLI

Accession

Primary (citable) accession number: P21170
Secondary accession number(s): Q2M9Q5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	August 29, 2003
Last modified:	September 2, 2008
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)