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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Prochlorococcus marinus (strain MIT 9515)
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:P9515_00521
OrganismiProchlorococcus marinus (strain MIT 9515)
Taxonomic identifieri167542 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesProchloraceaeProchlorococcus
Proteomesi
  • UP000001589 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000242601 – 648Biosynthetic arginine decarboxylaseAdd BLAST648

Amino acid modifications

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

Interactioni

Protein-protein interaction databases

STRINGi167542.P9515_00521.

Structurei

3D structure databases

ProteinModelPortaliA2BU00.
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.

A2BU00-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNFDSKKLN KHWTIEDSIS TYGIDKWGDQ YFSINSLGNI SITPNRNSKK
60 70 80 90 100
TIDLFKLVNE IKSREINTPL ILRFNDILKD RITELNNAFS QAIETYNYKN
110 120 130 140 150
IFQGVFPIKC NQQKNVLEKI IEYGDYWDFG LEVGSKSELL IGLSLLENKK
160 170 180 190 200
SLLICNGYKD KKYIEIAILA RKLGKQPIIV IEQIDEVQRI IEAVKNLRST
210 220 230 240 250
PILGIRSKLS SKSSGRWGKS VGDNSKFGLS IPEIMLTIKE LKEASLINEM
260 270 280 290 300
KLLHFHIGSQ ISDISVIKDA LQEASQIFVE LSKLGAPMKY IDVGGGLGID
310 320 330 340 350
FDGTKTSSNT STNYSLQNYA NDVVATIKDS CEVNNIQHPI IISESGRAIV
360 370 380 390 400
SHCSVLIFDV LGTSHVSSQI KVSHQKKTSL IIKNLIDTHN QLKNLRNKKE
410 420 430 440 450
DLSEIIELWN DAKKFKKDCL VAFRLGFISL GERAYAEELT WACAKEISSH
460 470 480 490 500
LDNEKIIHPD LSEITETLSS TYYANLSVFK SIPDTWAINQ IFPIIPIHRH
510 520 530 540 550
LEEPICKGNF ADLTCDSDGK LNNFIDNGKI KSLLNLHRPE ENNDYLIGIF
560 570 580 590 600
MAGAYQEALG NFHNLFGNTN VIHIDINEDN TYKIKNIIKE NSKSEILELL
610 620 630 640
DYSSDNLVES IRINTEFAIN NKTLSIEEAR KLIDQIETSL RKSSYLSE
Length:648
Mass (Da):73,324
Last modified:February 20, 2007 - v1
Checksum:iFAD4EF01EC8D33A4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000552 Genomic DNA. Translation: ABM71261.1.
RefSeqiWP_011819378.1. NC_008817.1.

Genome annotation databases

EnsemblBacteriaiABM71261; ABM71261; P9515_00521.
KEGGipmc:P9515_00521.
PATRICi23013618. VBIProMar113831_0054.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000552 Genomic DNA. Translation: ABM71261.1.
RefSeqiWP_011819378.1. NC_008817.1.

3D structure databases

ProteinModelPortaliA2BU00.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi167542.P9515_00521.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABM71261; ABM71261; P9515_00521.
KEGGipmc:P9515_00521.
PATRICi23013618. VBIProMar113831_0054.

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_PROM5
AccessioniPrimary (citable) accession number: A2BU00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 20, 2007
Last modified: November 2, 2016
This is version 66 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.