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A5GWM2

- SPEA_SYNR3

UniProt

A5GWM2 - SPEA_SYNR3

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Protein
Biosynthetic arginine decarboxylase
Gene
speA, SynRCC307_2378
Organism
Synechococcus sp. (strain RCC307)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the biosynthesis of agmatine from arginine By similarity.UniRule annotation

Catalytic activityi

L-arginine = agmatine + CO2.UniRule annotation

Cofactori

Magnesium By similarity.UniRule annotation
Pyridoxal phosphate By similarity.UniRule 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 decarboxylase (EC:4.1.1.19)
Short name:
ADC
Gene namesi
Name:speA
Ordered Locus Names:SynRCC307_2378
OrganismiSynechococcus sp. (strain RCC307)
Taxonomic identifieri316278 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000001115: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 640640Biosynthetic arginine decarboxylaseUniRule annotation
PRO_1000024276Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei109 – 1091N6-(pyridoxal phosphate)lysine By similarity

Interactioni

Protein-protein interaction databases

STRINGi316278.SynRCC307_2378.

Structurei

3D structure databases

ProteinModelPortaliA5GWM2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni291 – 30111Substrate-binding Reviewed prediction
Add
BLAST

Sequence similaritiesi

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

MVVAPSQVEQ QNWTPAASAQ LYGLDQWGDP YFSVNARGHV LVQPRGDRGG    50
SLDLVELVEG LQSRDLQLPL LIRFEDILED RLERLHGAFE RAIAQYGYGG 100
HYQGVFPVKC NQQRHVVEQL VESGRRWHFG LEAGSKAELL IALSLLDDPK 150
ALLICNGYKD QRYIETAILA RQLGRQPVVV IEQADEVPRI IEASRNLGAA 200
PLIGVRAKLS TRSTGRWGSS VGEKAKFGLS IPDLLATVEA LRDADLLGDL 250
RLLHFHVGSQ ICDIAVLKDA LQEAGQLYVQ LASLGAPMGF LDVGGGLGVD 300
YDGSRSATAA STNYSLQNYA NDVVATIREC CEPQGIVVPT LVSESGRAIA 350
SHFSVLVFNV LGQSGVNQPS IPEAVEGEAL IVRNLRETLS GIGPDNLQEA 400
WNDALKFKDD ALAAFRLGYL SLTERGKAEQ LYWACCSAIA DLLPGEEELP 450
DELKGLKAAF ASTYYANLSV FRSAPDTWAI DQLFPVMPIH RLEEQPRELG 500
SFADLTCDSD GKLARFIASG SAKPLLELHE LKDGEPYWIG LFLGGAYQEV 550
MGNLHNLFGS TNAVSIRLSP GGPYRVEHVV RGQTNSDVLE AMEHNPEALL 600
ERLRQASEEA IGSGDLSISA ARRLMQHLEG SLRQTTYLEE 640
Length:640
Mass (Da):69,862
Last modified:June 12, 2007 - v1
Checksum:iB62EFE2DF8DD1705
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
GeneIDi5156587.
KEGGisyr:SynRCC307_2378.
PATRICi23825709. VBISynSp108374_2389.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CT978603 Genomic DNA. Translation: CAK29281.1 .
RefSeqi WP_011936790.1. NC_009482.1.
YP_001228634.1. NC_009482.1.

3D structure databases

ProteinModelPortali A5GWM2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 316278.SynRCC307_2378.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAK29281 ; CAK29281 ; SynRCC307_2378 .
GeneIDi 5156587.
KEGGi syr:SynRCC307_2378.
PATRICi 23825709. VBISynSp108374_2389.

Phylogenomic databases

eggNOGi COG1166.
HOGENOMi HOG000029191.
KOi K01585.
OMAi IDHYVDG.
OrthoDBi EOG676Z0R.

Enzyme and pathway databases

UniPathwayi UPA00186 ; UER00284 .

Family and domain databases

Gene3Di 2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
HAMAPi MF_01417. SpeA.
InterProi IPR009006. 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 ]
Pfami PF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view ]
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 PS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 51 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

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