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 + CO2. HAMAP MF_01417
Cofactor	Pyridoxal phosphate. HAMAP MF_01417 Magnesium. HAMAP MF_01417
Pathway	Amino-acid degradation; L-arginine degradation via ADC pathway; agmatine from L-arginine: step 1/1. HAMAP MF_01417
Subunit structure	Homotetramer. HAMAP MF_01417
Subcellular location	Periplasm. Ref.1
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. HAMAP MF_01417
Post-translational modification	Processed post-translationally to a 70 kDa mature form. HAMAP MF_01417 The N-terminus is blocked. HAMAP MF_01417
Miscellaneous	ADC can be found in two forms: biodegradative and biosynthetic. The biodegradative form may play a role in regulating pH by consuming proteins. HAMAP MF_01417
Sequence similarities	Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily.
Biophysicochemical properties	pH dependence: Optimum pH is 8.4. HAMAP MF_01417

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	arginine catabolic process Inferred from electronic annotation. Source: InterPro putrescine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW spermidine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	arginine decarboxylase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 658	658	Biosynthetic arginine decarboxylase HAMAP MF_01417		PRO_0000149960
Regions
	Region	307 – 317	11	Substrate-binding Potential
Amino acid modifications
	Modified residue	127	1	N6-(pyridoxal phosphate)lysine 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.
Genome annotation databases
GeneID	947432.
GenomeReviews	Gene locus JW2905 in contig AP009048_GR. Gene locus b2938 in contig U00096_GR.
KEGG	ecj:JW2905. eco:b2938.
Organism-specific databases
EchoBASE	EB0952.
EcoGene	EG10959. speA.
CMR	Search...
Phylogenomic databases
HOGENOM	P21170.
OMA	P21170. LICNGYK.
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]
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:	June 16, 2009
This is version 89 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)