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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Prochlorococcus marinus (strain MIT 9215)
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

Pathway: 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

BioCyciPMAR93060:GI08-57-MONOMER.
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:P9215_00551
OrganismiProchlorococcus marinus (strain MIT 9215)
Taxonomic identifieri93060 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000002014 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 648648Biosynthetic arginine decarboxylasePRO_1000068493Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei109 – 1091N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi93060.P9215_00551.

Structurei

3D structure databases

ProteinModelPortaliA8G243.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni291 – 30111Substrate-bindingUniRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
KOiK01585.
OMAiIDHYVDG.
OrthoDBiEOG676Z0R.

Family and domain databases

Gene3Di2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
HAMAPiMF_01417. SpeA.
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. 1 hit.
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.

A8G243-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNFEPKKLK KNWTIEDSIS TYEIDKWGDK YFSINSKGNI SVTKDINSEK
60 70 80 90 100
KIDLFKLVRE LKSREINTPL IIRFNDILKD RINALHDAFL KAIKTYKYKN
110 120 130 140 150
IYQGVFPVKC NQQKNVLEKI IEFGSPWNFG LEVGSKSELL IGLALLENQN
160 170 180 190 200
SLLICNGYKD KKYIEIATLA RKLGKNPIIV IEQKDEVNRI IEAVQDLNAS
210 220 230 240 250
PLIGIRAKLS SKSSGRWSKS VGDNSKFGLS IPEIMSTIKE LKEANLINEM
260 270 280 290 300
RLLHFHIGSQ ISDIAVIKDA LQEASQIYVE LFKLGAPMKY IDVGGGLGID
310 320 330 340 350
FDGTKTSSNT STNYSLQNYA NDVIATIKDS CELNNIEHPT IISESGRAII
360 370 380 390 400
SHCSVLIFNV LGTSHVSSKL KIYDDKKQSL IISNLIETFY ELKKLKNKKI
410 420 430 440 450
NLSQIIELWN DAKKFKEDCL VAFRLGFLSL AERAYAEELT WACAKEIANN
460 470 480 490 500
LNNDEINHPD LFEITETLAS TYYANLSIFK SIPDCWAINQ IFPIMPIHRH
510 520 530 540 550
LEEPFCKGNF ADLTCDSDGK LNSFINNGKI KSLLNLHEPE QDKDYLIGIF
560 570 580 590 600
MTGAYQEALG NLHNLFGNTN VVHIDINQND SYKVKNIIKE DSKSEILQLL
610 620 630 640
DYSSASLVES IRINTEAAID QKKLTIEEAR KLIDQIEISL RKSSYLSE
Length:648
Mass (Da):73,405
Last modified:November 13, 2007 - v1
Checksum:i3472447352E0C4E6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000825 Genomic DNA. Translation: ABV49674.1.
RefSeqiWP_012006859.1. NC_009840.1.
YP_001483260.1. NC_009840.1.

Genome annotation databases

EnsemblBacteriaiABV49674; ABV49674; P9215_00551.
KEGGipmh:P9215_00551.
PATRICi22989523. VBIProMar119824_0056.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000825 Genomic DNA. Translation: ABV49674.1.
RefSeqiWP_012006859.1. NC_009840.1.
YP_001483260.1. NC_009840.1.

3D structure databases

ProteinModelPortaliA8G243.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93060.P9215_00551.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABV49674; ABV49674; P9215_00551.
KEGGipmh:P9215_00551.
PATRICi22989523. VBIProMar119824_0056.

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
KOiK01585.
OMAiIDHYVDG.
OrthoDBiEOG676Z0R.

Enzyme and pathway databases

UniPathwayiUPA00186; UER00284.
BioCyciPMAR93060:GI08-57-MONOMER.

Family and domain databases

Gene3Di2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
HAMAPiMF_01417. SpeA.
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. 1 hit.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MIT 9215.

Entry informationi

Entry nameiSPEA_PROM2
AccessioniPrimary (citable) accession number: A8G243
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 13, 2007
Last modified: June 24, 2015
This is version 59 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

External Data

Dasty 3

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 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.