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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Synechococcus sp. (strain RCC307)
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

GO - Molecular functioni

  1. arginine decarboxylase activity Source: UniProtKB-HAMAP
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. arginine catabolic process Source: InterPro
  2. spermidine biosynthetic process Source: UniProtKB-HAMAP
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:SynRCC307_2378
OrganismiSynechococcus sp. (strain RCC307)
Taxonomic identifieri316278 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000001115 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 640640Biosynthetic arginine decarboxylasePRO_1000024276Add
BLAST

Amino acid modifications

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

Interactioni

Protein-protein interaction databases

STRINGi316278.SynRCC307_2378.

Structurei

3D structure databases

ProteinModelPortaliA5GWM2.
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]
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.

A5GWM2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVAPSQVEQ QNWTPAASAQ LYGLDQWGDP YFSVNARGHV LVQPRGDRGG
60 70 80 90 100
SLDLVELVEG LQSRDLQLPL LIRFEDILED RLERLHGAFE RAIAQYGYGG
110 120 130 140 150
HYQGVFPVKC NQQRHVVEQL VESGRRWHFG LEAGSKAELL IALSLLDDPK
160 170 180 190 200
ALLICNGYKD QRYIETAILA RQLGRQPVVV IEQADEVPRI IEASRNLGAA
210 220 230 240 250
PLIGVRAKLS TRSTGRWGSS VGEKAKFGLS IPDLLATVEA LRDADLLGDL
260 270 280 290 300
RLLHFHVGSQ ICDIAVLKDA LQEAGQLYVQ LASLGAPMGF LDVGGGLGVD
310 320 330 340 350
YDGSRSATAA STNYSLQNYA NDVVATIREC CEPQGIVVPT LVSESGRAIA
360 370 380 390 400
SHFSVLVFNV LGQSGVNQPS IPEAVEGEAL IVRNLRETLS GIGPDNLQEA
410 420 430 440 450
WNDALKFKDD ALAAFRLGYL SLTERGKAEQ LYWACCSAIA DLLPGEEELP
460 470 480 490 500
DELKGLKAAF ASTYYANLSV FRSAPDTWAI DQLFPVMPIH RLEEQPRELG
510 520 530 540 550
SFADLTCDSD GKLARFIASG SAKPLLELHE LKDGEPYWIG LFLGGAYQEV
560 570 580 590 600
MGNLHNLFGS TNAVSIRLSP GGPYRVEHVV RGQTNSDVLE AMEHNPEALL
610 620 630 640
ERLRQASEEA IGSGDLSISA ARRLMQHLEG SLRQTTYLEE
Length:640
Mass (Da):69,862
Last modified:June 12, 2007 - v1
Checksum:iB62EFE2DF8DD1705
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CT978603 Genomic DNA. Translation: CAK29281.1.
RefSeqiWP_011936790.1. NC_009482.1.
YP_001228634.1. NC_009482.1.

Genome annotation databases

EnsemblBacteriaiCAK29281; CAK29281; SynRCC307_2378.
KEGGisyr:SynRCC307_2378.
PATRICi23825709. VBISynSp108374_2389.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CT978603 Genomic DNA. Translation: CAK29281.1.
RefSeqiWP_011936790.1. NC_009482.1.
YP_001228634.1. NC_009482.1.

3D structure databases

ProteinModelPortaliA5GWM2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi316278.SynRCC307_2378.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAK29281; CAK29281; SynRCC307_2378.
KEGGisyr:SynRCC307_2378.
PATRICi23825709. VBISynSp108374_2389.

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
KOiK01585.
OMAiIDHYVDG.
OrthoDBiEOG676Z0R.

Enzyme and pathway databases

UniPathwayiUPA00186; UER00284.

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]
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. Genoscope
    Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RCC307.

Entry informationi

Entry nameiSPEA_SYNR3
AccessioniPrimary (citable) accession number: A5GWM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 12, 2007
Last modified: April 29, 2015
This is version 55 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, Reference 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.