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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Prochlorococcus marinus (strain MIT 9301)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the biosynthesis of agmatine from arginine.UniRule annotation

Catalytic activityi

L-arginine = agmatine + CO2.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotation
  • pyridoxal 5'-phosphateUniRule annotation

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:
  1. 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Polyamine biosynthesis, Spermidine biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00186; 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
Ordered Locus Names:P9301_00481
OrganismiProchlorococcus marinus (strain MIT 9301)
Taxonomic identifieri167546 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesProchloraceaeProchlorococcus
Proteomesi
  • UP000001430 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000242581 – 648Biosynthetic arginine decarboxylaseAdd BLAST648

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei109N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Protein-protein interaction databases

STRINGi167546.P9301_00481.

Structurei

3D structure databases

ProteinModelPortaliA3PA96.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni291 – 301Substrate-bindingUniRule annotationAdd BLAST11

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105DP5. Bacteria.
COG1166. LUCA.
HOGENOMiHOG000029191.
KOiK01585.
OMAiDQLFPIM.
OrthoDBiPOG091H04NG.

Family and domain databases

CDDicd06830. PLPDE_III_ADC. 1 hit.
Gene3Di2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
HAMAPiMF_01417. SpeA. 1 hit.
InterProiIPR009006. 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.
IPR029066. PLP-binding_barrel.
[Graphical view]
PANTHERiPTHR11482:SF36. PTHR11482:SF36. 2 hits.
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PIRSFiPIRSF001336. Arg_decrbxlase. 1 hit.
PRINTSiPR01180. ARGDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR01273. speA. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A3PA96-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNFEPKKLK NVWTIEDSIS TYNIDKWGDK YFSINSKGNI SVTKDIKSEN
60 70 80 90 100
KIDLFKLVKE LKSREINPPL IIRFNDILKD RINALHDSFF KAIKTYKYKN
110 120 130 140 150
IYQGVFPVKC NQQKNVLEKI IDFGSQWNFG LEVGSKSELL IGLALLENHN
160 170 180 190 200
SLLICNGYKD KKYIEIATLA RKLGKNPIIV IEQRDEVKRI IQAVQELNAT
210 220 230 240 250
PLIGIRAKLS SKSSGRWGKS IGDNSKFGLS IPEIMLTIKE LKEANLINEM
260 270 280 290 300
KLLHFHIGSQ ISDIAVIKDA LQEASQIYVE LCKLGAPMQY IDVGGGLGID
310 320 330 340 350
FDGTKTSSNT STNYSLQNYA NDVIATIKDS CELNNIKHPT IISESGRAII
360 370 380 390 400
SHCSVLIFNV LGTSHVSSKL QIFDKKNQQL IISNLLETYY ELKKLKNKKI
410 420 430 440 450
NLSQIIELWN DAKKFKEDCL VAFRLGFLSL AERAYAEELA WACAKEISNN
460 470 480 490 500
LNNDEINHPD LSEITETLAS TYYANLSIFK SIPDSWAINQ IFPIVPIHRH
510 520 530 540 550
LEEPFCKGNF ADLTCDSDGK LNNFIDDGKI KSLLNLHEPE KDKDYLIGIF
560 570 580 590 600
MTGAYQEALG NLHNLFGSTN VVHIDINQDD SYKVKNIIKE DSKSEILQLL
610 620 630 640
DYSSASLVES IRINTESAID QKKLTIEEAR KLMDQIEISL RKSSYLSE
Length:648
Mass (Da):73,366
Last modified:April 3, 2007 - v1
Checksum:i7B3791D58CCC947E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000576 Genomic DNA. Translation: ABO16671.1.
RefSeqiWP_011862076.1. NC_009091.1.

Genome annotation databases

EnsemblBacteriaiABO16671; ABO16671; P9301_00481.
KEGGipmg:P9301_00481.
PATRICi22993689. VBIProMar103344_0049.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000576 Genomic DNA. Translation: ABO16671.1.
RefSeqiWP_011862076.1. NC_009091.1.

3D structure databases

ProteinModelPortaliA3PA96.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi167546.P9301_00481.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABO16671; ABO16671; P9301_00481.
KEGGipmg:P9301_00481.
PATRICi22993689. VBIProMar103344_0049.

Phylogenomic databases

eggNOGiENOG4105DP5. Bacteria.
COG1166. LUCA.
HOGENOMiHOG000029191.
KOiK01585.
OMAiDQLFPIM.
OrthoDBiPOG091H04NG.

Enzyme and pathway databases

UniPathwayiUPA00186; UER00284.

Family and domain databases

CDDicd06830. PLPDE_III_ADC. 1 hit.
Gene3Di2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
HAMAPiMF_01417. SpeA. 1 hit.
InterProiIPR009006. 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.
IPR029066. PLP-binding_barrel.
[Graphical view]
PANTHERiPTHR11482:SF36. PTHR11482:SF36. 2 hits.
PfamiPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PIRSFiPIRSF001336. Arg_decrbxlase. 1 hit.
PRINTSiPR01180. ARGDCRBXLASE.
PR01179. ODADCRBXLASE.
SUPFAMiSSF50621. SSF50621. 1 hit.
SSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR01273. speA. 1 hit.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSPEA_PROM0
AccessioniPrimary (citable) accession number: A3PA96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 3, 2007
Last modified: November 2, 2016
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.