Q8FE34 (SPEA_ECOL6) Reviewed, UniProtKB/Swiss-Prot

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:	c3524

Organism

Escherichia coli O6 [Complete proteome] [HAMAP]

Taxonomic identifier

217992 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	658 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the biosynthesis of agmatine from arginine By similarity. HAMAP MF_01417
Catalytic activity	L-arginine = agmatine + CO2. HAMAP MF_01417
Cofactor	Magnesium By similarity. HAMAP MF_01417 Pyridoxal phosphate By similarity. HAMAP MF_01417
Pathway	Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1. HAMAP MF_01417
Subunit structure	Homotetramer By similarity. HAMAP MF_01417
Subcellular location	Periplasm By similarity HAMAP MF_01417.
Sequence similarities	Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily.
Sequence caution	The sequence AAN81972.1 differs from that shown. Reason: Erroneous initiation.

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: UniProtKB-KW
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	arginine decarboxylase activity Inferred from electronic annotation. Source: EC metal 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_0000149961
Regions
	Region	307 – 317	11	Substrate-binding Potential
Amino acid modifications
	Modified residue	127	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8FE34 [UniParc]. Last modified March 29, 2004. Version 2. Checksum: 87106BF8727B6EE2	FASTA	658	73,886
	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 IHIGYSSGTF 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

[1]

"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014075 Genomic DNA. Translation: AAN81972.1. Different initiation.
RefSeq	NP_755399.1. NC_004431.1.
3D structure databases
ProteinModelPortal	Q8FE34.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000042067; EBESCP00000040416; EBESCG00000041117.
GeneID	1039437.
GenomeReviews	Gene locus c3524 in contig AE014075_GR.
KEGG	ecc:c3524.
PATRIC	18284870. VBIEscCol75197_3320.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000009574.
HOGENOM	HBG321436.
OMA	LICNGYK.
ProtClustDB	PRK05354.
Family and domain databases
HAMAP	MF_01417. SpeA. [Tree]
InterPro	IPR009006. Ala_racemase/Decarboxylase_C. IPR002985. Arg_decrbxlase. IPR022643. De-COase2_C. IPR022657. De-COase2_CS. IPR022644. De-COase2_N. IPR022653. De-COase2_pyr-phos_BS. IPR000183. Orn/DAP/Arg_de-COase. [Graphical view]
Gene3D	G3DSA:2.40.37.10. Ala_racemase/Decarboxylase_C. 2 hits.
KO	K01585.
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.
SUPFAM	SSF50621. Racem_decarbox_C. 1 hit.
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_ECOL6

Accession

Primary (citable) accession number: Q8FE34

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2004
Last sequence update:	March 29, 2004
Last modified:	January 25, 2012
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program