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UniProtKB - P21170 (SPEA_ECOLI)
Protein
Biosynthetic arginine decarboxylase
Gene
speA
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the biosynthesis of agmatine from arginine.
3 PublicationsMiscellaneous
ADC can be found in two forms: biodegradative and biosynthetic. The biodegradative form may play a role in regulating pH by consuming proteins.
Catalytic activityi
Cofactori
Protein has several cofactor binding sites:- pyridoxal 5'-phosphate
- Mg2+1 Publication
Activity regulationi
Down-regulated by polyamine end products putrescine and spermidine.1 Publication
Kineticsi
- KM=0.03 mM for L-arginine1 Publication
pH dependencei
Optimum pH is 8.4.1 Publication
Temperature dependencei
Optimum temperature is 50 degrees Celsius. Thermostable. Active from 20 to 80 degrees Celsius.1 Publication
: agmatine biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes agmatine from L-arginine.1 Publication This subpathway is part of the pathway agmatine biosynthesis, which is itself part of Amine and polyamine biosynthesis.View all proteins of this organism that are known to be involved in the subpathway that synthesizes agmatine from L-arginine, the pathway agmatine biosynthesis and in Amine and polyamine biosynthesis.
GO - Molecular functioni
- arginine decarboxylase activity Source: EcoCyc
- identical protein binding Source: EcoCyc
- magnesium ion binding Source: EcoCyc
- pyridoxal phosphate binding Source: EcoCyc
GO - Biological processi
- arginine catabolic process Source: EcoCyc
- protein homotetramerization Source: EcoCyc
- putrescine biosynthetic process Source: EcoCyc
- putrescine biosynthetic process from arginine Source: EcoCyc
- spermidine biosynthetic process Source: UniProtKB-UniRule
Keywordsi
Molecular function | Decarboxylase, Lyase |
Biological process | Polyamine biosynthesis, Putrescine biosynthesis, Spermidine biosynthesis |
Ligand | Magnesium, Metal-binding, Pyridoxal phosphate |
Enzyme and pathway databases
BioCyci | EcoCyc:ARGDECARBOXBIO-MONOMER |
BRENDAi | 4.1.1.19, 2026 |
SABIO-RKi | P21170 |
UniPathwayi | UPA00186;UER00284 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:speA Ordered Locus Names:b2938, JW2905 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Other locations
- Periplasm 1 Publication
Other locations
- periplasmic space Source: UniProtKB-SubCell
Keywords - Cellular componenti
PeriplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000149960 | 1 – 658 | Biosynthetic arginine decarboxylaseAdd BLAST | 658 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 127 | N6-(pyridoxal phosphate)lysineBy similarity | 1 |
Post-translational modificationi
Processed post-translationally to a 70 kDa mature form.
The N-terminus is blocked.
Proteomic databases
jPOSTi | P21170 |
PaxDbi | P21170 |
PRIDEi | P21170 |
Expressioni
Inductioni
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.
Interactioni
Subunit structurei
Homotetramer.
1 PublicationGO - Molecular functioni
- identical protein binding Source: EcoCyc
Protein-protein interaction databases
BioGRIDi | 4262346, 13 interactors 851752, 4 interactors |
DIPi | DIP-10905N |
IntActi | P21170, 16 interactors |
STRINGi | 511145.b2938 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | P21170 |
SMRi | P21170 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P21170 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 307 – 317 | Substrate-bindingSequence analysisAdd BLAST | 11 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG1166, Bacteria |
HOGENOMi | CLU_027243_1_0_6 |
InParanoidi | P21170 |
OMAi | AVEYTQH |
PhylomeDBi | P21170 |
Family and domain databases
CDDi | cd06830, PLPDE_III_ADC, 1 hit |
Gene3Di | 2.40.37.10, 1 hit 3.20.20.10, 1 hit |
HAMAPi | MF_01417, SpeA, 1 hit |
InterProi | View protein in InterPro IPR009006, Ala_racemase/Decarboxylase_C IPR040634, Arg_decarb_HB IPR041128, Arg_decarbox_C IPR002985, Arg_decrbxlase IPR022657, De-COase2_CS IPR022644, De-COase2_N IPR022653, De-COase2_pyr-phos_BS IPR000183, Orn/DAP/Arg_de-COase IPR029066, PLP-binding_barrel |
PANTHERi | PTHR43295, PTHR43295, 1 hit |
Pfami | View protein in Pfam PF17810, Arg_decarb_HB, 1 hit PF17944, Arg_decarbox_C, 1 hit PF02784, Orn_Arg_deC_N, 1 hit |
PIRSFi | PIRSF001336, Arg_decrbxlase, 1 hit |
PRINTSi | PR01180, ARGDCRBXLASE PR01179, ODADCRBXLASE |
SUPFAMi | SSF50621, SSF50621, 1 hit SSF51419, SSF51419, 1 hit |
TIGRFAMsi | TIGR01273, speA, 1 hit |
PROSITEi | View protein in PROSITE PS00878, ODR_DC_2_1, 1 hit PS00879, ODR_DC_2_2, 1 hit |
i Sequence
Sequence statusi: Complete.
P21170-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSDDMSMGLP SSAGEHGVLR SMQEVAMSSQ EASKMLRTYN IAWWGNNYYD
60 70 80 90 100
VNELGHISVC PDPDVPEARV DLAQLVKTRE AQGQRLPALF CFPQILQHRL
110 120 130 140 150
RSINAAFKRA RESYGYNGDY FLVYPIKVNQ HRRVIESLIH SGEPLGLEAG
160 170 180 190 200
SKAELMAVLA HAGMTRSVIV CNGYKDREYI RLALIGEKMG HKVYLVIEKM
210 220 230 240 250
SEIAIVLDEA ERLNVVPRLG VRARLASQGS GKWQSSGGEK SKFGLAATQV
260 270 280 290 300
LQLVETLREA GRLDSLQLLH FHLGSQMANI RDIATGVRES ARFYVELHKL
310 320 330 340 350
GVNIQCFDVG GGLGVDYEGT RSQSDCSVNY GLNEYANNII WAIGDACEEN
360 370 380 390 400
GLPHPTVITE SGRAVTAHHT VLVSNIIGVE RNEYTVPTAP AEDAPRALQS
410 420 430 440 450
MWETWQEMHE PGTRRSLREW LHDSQMDLHD IHIGYSSGIF SLQERAWAEQ
460 470 480 490 500
LYLSMCHEVQ KQLDPQNRAH RPIIDELQER MADKMYVNFS LFQSMPDAWG
510 520 530 540 550
IDQLFPVLPL EGLDQVPERR AVLLDITCDS DGAIDHYIDG DGIATTMPMP
560 570 580 590 600
EYDPENPPML GFFMVGAYQE ILGNMHNLFG DTEAVDVFVF PDGSVEVELS
610 620 630 640 650
DEGDTVADML QYVQLDPKTL LTQFRDQVKK TDLDAELQQQ FLEEFEAGLY
GYTYLEDE
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 226 | A → R in AAA24646 (PubMed:2198270).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | 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. |
PIRi | A65079 |
RefSeqi | NP_417413.1, NC_000913.3 WP_001300904.1, NZ_SSZK01000003.1 |
Genome annotation databases
EnsemblBacteriai | AAC75975; AAC75975; b2938 BAE77001; BAE77001; BAE77001 |
GeneIDi | 947432 |
KEGGi | ecj:JW2905 eco:b2938 |
PATRICi | fig|1411691.4.peg.3795 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | 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. |
PIRi | A65079 |
RefSeqi | NP_417413.1, NC_000913.3 WP_001300904.1, NZ_SSZK01000003.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3NZQ | X-ray | 3.10 | A/B | 1-658 | [»] | |
AlphaFoldDBi | P21170 | |||||
SMRi | P21170 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4262346, 13 interactors 851752, 4 interactors |
DIPi | DIP-10905N |
IntActi | P21170, 16 interactors |
STRINGi | 511145.b2938 |
Proteomic databases
jPOSTi | P21170 |
PaxDbi | P21170 |
PRIDEi | P21170 |
Protocols and materials databases
DNASUi | 947432 |
Genome annotation databases
EnsemblBacteriai | AAC75975; AAC75975; b2938 BAE77001; BAE77001; BAE77001 |
GeneIDi | 947432 |
KEGGi | ecj:JW2905 eco:b2938 |
PATRICi | fig|1411691.4.peg.3795 |
Organism-specific databases
EchoBASEi | EB0952 |
Phylogenomic databases
eggNOGi | COG1166, Bacteria |
HOGENOMi | CLU_027243_1_0_6 |
InParanoidi | P21170 |
OMAi | AVEYTQH |
PhylomeDBi | P21170 |
Enzyme and pathway databases
UniPathwayi | UPA00186;UER00284 |
BioCyci | EcoCyc:ARGDECARBOXBIO-MONOMER |
BRENDAi | 4.1.1.19, 2026 |
SABIO-RKi | P21170 |
Miscellaneous databases
EvolutionaryTracei | P21170 |
PROi | PR:P21170 |
Family and domain databases
CDDi | cd06830, PLPDE_III_ADC, 1 hit |
Gene3Di | 2.40.37.10, 1 hit 3.20.20.10, 1 hit |
HAMAPi | MF_01417, SpeA, 1 hit |
InterProi | View protein in InterPro IPR009006, Ala_racemase/Decarboxylase_C IPR040634, Arg_decarb_HB IPR041128, Arg_decarbox_C IPR002985, Arg_decrbxlase IPR022657, De-COase2_CS IPR022644, De-COase2_N IPR022653, De-COase2_pyr-phos_BS IPR000183, Orn/DAP/Arg_de-COase IPR029066, PLP-binding_barrel |
PANTHERi | PTHR43295, PTHR43295, 1 hit |
Pfami | View protein in Pfam PF17810, Arg_decarb_HB, 1 hit PF17944, Arg_decarbox_C, 1 hit PF02784, Orn_Arg_deC_N, 1 hit |
PIRSFi | PIRSF001336, Arg_decrbxlase, 1 hit |
PRINTSi | PR01180, ARGDCRBXLASE PR01179, ODADCRBXLASE |
SUPFAMi | SSF50621, SSF50621, 1 hit SSF51419, SSF51419, 1 hit |
TIGRFAMsi | TIGR01273, speA, 1 hit |
PROSITEi | View protein in PROSITE PS00878, ODR_DC_2_1, 1 hit PS00879, ODR_DC_2_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | SPEA_ECOLI | |
Accessioni | P21170Primary (citable) accession number: P21170 Secondary accession number(s): Q2M9Q5 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 1, 1991 |
Last sequence update: | August 29, 2003 | |
Last modified: | May 25, 2022 | |
This is version 179 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families