speA

Functionⁱ

Catalyzes the biosynthesis of agmatine from arginine.UniRule annotation

Catalytic activityⁱ

L-arginine = agmatine + CO₂.UniRule annotationSAAS annotation

Cofactorⁱ

Protein has several cofactor binding sites:

Mg²⁺
UniRule annotation
Automatic assertion according to rulesⁱ
- HAMAP-Rule:MF_01417
SAAS annotation
Automatic assertion according to rulesⁱ
- SAAS:SAAS00722737
pyridoxal 5'-phosphate
UniRule annotation
Automatic assertion according to rulesⁱ
- HAMAP-Rule:MF_01417
- PIRSR:PIRSR001336-50
SAAS annotation
Automatic assertion according to rulesⁱ
- SAAS:SAAS00758845

Pathwayⁱ: agmatine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes agmatine from L-arginine.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:

Biosynthetic arginine decarboxylase (speA), Biosynthetic arginine decarboxylase (speA), Biosynthetic arginine decarboxylase (speA)

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: UniProtKB-UniRule
metal ion binding Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

arginine catabolic process Source: InterPro
putrescine biosynthetic process Source: UniProtKB-UniRule
spermidine biosynthetic process Source: UniProtKB-UniRule

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DecarboxylaseUniRule annotationSAAS annotation, Lyase
Biological process	Polyamine biosynthesisUniRule annotation, Putrescine biosynthesisUniRule annotation, Spermidine biosynthesisUniRule annotationSAAS annotation
Ligand	MagnesiumUniRule annotationSAAS annotation, Metal-bindingUniRule annotation, Pyridoxal phosphateUniRule annotationSAAS annotation

Enzyme and pathway databases

UniPathwayⁱ	UPA00186; UER00284.

UniPathwayⁱ

UPA00186; UER00284.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Biosynthetic arginine decarboxylaseUniRule annotation (EC:4.1.1.19UniRule annotation) Short name: ADCUniRule annotation
Gene namesⁱ	Name:speAUniRule annotation ORF Names:CI726_29125Imported
Organismⁱ	Shigella sonneiImported
Taxonomic identifierⁱ	624 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Shigella
Proteomesⁱ	UP000215054 Componentⁱ: Unassembled WGS sequence

PTM / Processingⁱ

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	127	N6-(pyridoxal phosphate)lysineUniRule annotation		1

Structureⁱ

3D structure databases

SMRⁱ	A0A236Q3T9.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	307 – 317	Substrate-bindingUniRule annotationAdd BLAST		11

Sequence similaritiesⁱ

Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily.UniRule annotationSAAS annotation

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd06830. PLPDE_III_ADC. 1 hit.
Gene3Dⁱ	2.40.37.10. 3 hits. 3.20.20.10. 1 hit.
HAMAPⁱ	MF_01417. SpeA. 1 hit.
InterProⁱ	View protein in InterPro IPR009006. Ala_racemase/Decarboxylase_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.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam 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.

Sequenceⁱ

Sequence statusⁱ: Complete.

A0A236Q3T9-1 [UniParc]FASTA Add to basket

« Hide

        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

Length:658

Mass (Da):73,898

Last modified:October 25, 2017 - v1

Checksum:ⁱ22613CEA5F957CC3

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	NQBH01000350 Genomic DNA. Translation: OYG90263.1.
NCBI Reference Sequences More...RefSeqⁱ	WP_001300904.1. NZ_NVQG01000033.1.

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
A0A236Q3T9	P21170 A0A094VSI0 A0A236GX33 F4SPL0 D7YB89 A0A140N5H6 A0A1X3JEB5 L2VFL1 A0A142H6E2 A0A0E1M1C6 +24	Escherichia coli (strain K12) Escherichia coli Shigella boydii Escherichia coli H736 Escherichia coli MS 115-1 Escherichia coli (strain B / BL21-DE3) Escherichia coli H386 Escherichia coli KTE10 Shigella sp. PAMC 28760 Escherichia coli 1303 And more	658	UniRef100_P21170	Cluster: Biosynthetic arginine decarboxylase	35

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
A0A236Q3T9	P21170 A0A094VSI0 A0A236GX33 F4SPL0 D7YB89 A0A140N5H6 A0A1X3JEB5 L2VFL1 A0A142H6E2 A0A0E1M1C6 +1080	Escherichia coli (strain K12) Escherichia coli Shigella boydii Escherichia coli H736 Escherichia coli MS 115-1 Escherichia coli (strain B / BL21-DE3) Escherichia coli H386 Escherichia coli KTE10 Shigella sp. PAMC 28760 Escherichia coli 1303 And more	658	UniRef90_P21170	Cluster: Biosynthetic arginine decarboxylase	1,091

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
A0A236Q3T9	P21170 A0A094VSI0 A0A236GX33 F4SPL0 D7YB89 A0A140N5H6 A0A1X3JEB5 L2VFL1 A0A142H6E2 A0A0E1M1C6 +1783	Escherichia coli (strain K12) Escherichia coli Shigella boydii Escherichia coli H736 Escherichia coli MS 115-1 Escherichia coli (strain B / BL21-DE3) Escherichia coli H386 Escherichia coli KTE10 Shigella sp. PAMC 28760 Escherichia coli 1303 And more	658	UniRef50_P21170	Cluster: Biosynthetic arginine decarboxylase	1,794

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	NQBH01000350 Genomic DNA. Translation: OYG90263.1.
NCBI Reference Sequences More...RefSeqⁱ	WP_001300904.1. NZ_NVQG01000033.1.

3D structure databases

SMRⁱ	A0A236Q3T9.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Enzyme and pathway databases

UniPathwayⁱ	UPA00186; UER00284.

UniPathwayⁱ

UPA00186; UER00284.

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd06830. PLPDE_III_ADC. 1 hit.
Gene3Dⁱ	2.40.37.10. 3 hits. 3.20.20.10. 1 hit.
HAMAPⁱ	MF_01417. SpeA. 1 hit.
InterProⁱ	View protein in InterPro IPR009006. Ala_racemase/Decarboxylase_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.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam 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.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	A0A236Q3T9_SHISO
Accessionⁱ	A0A236Q3T9Primary (citable) accession number: A0A236Q3T9
Entry historyⁱ	Integrated into UniProtKB/TrEMBL:	October 25, 2017
	Last sequence update:	October 25, 2017
	Last modified:	February 28, 2018
	This is version 5 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Unreviewed (UniProtKB/TrEMBL)

Miscellaneousⁱ

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

Keywords - Technical termⁱ

Complete proteomeImported

UniProtKB - A0A236Q3T9 (A0A236Q3T9_SHISO)

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Biosynthetic arginine decarboxylase

Select a section on the left to see content.

Functionⁱ

Catalytic activityⁱ

Cofactorⁱ

Pathwayⁱ: agmatine biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Keywordsⁱ

Enzyme and pathway databases

Names & Taxonomyⁱ

PTM / Processingⁱ

Amino acid modifications

Structureⁱ

3D structure databases

Family & Domainsⁱ

Region

Sequence similaritiesⁱ

Family and domain databases

Sequenceⁱ

Sequence databases

Similar proteinsⁱ

Cross-referencesⁱ

Sequence databases

3D structure databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

Entry informationⁱ

Miscellaneousⁱ

Caution

Keywords - Technical termⁱ

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - A0A236Q3T9 (A0A236Q3T9_SHISO)

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Biosynthetic arginine decarboxylase

speA

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">‘Function’</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: agmatine biosynthesis

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Amino acid modifications

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Family and domain databases

Sequence databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Caution

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Functionⁱ

Pathwayⁱ: agmatine biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

PTM / Processingⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ