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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Synechococcus sp. (strain WH8102)
Status
Reviewed-Annotation score: Annotation score: 2 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

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

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:SYNW2359
OrganismiSynechococcus sp. (strain WH8102)
Taxonomic identifieri84588 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000001422 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 644644Biosynthetic arginine decarboxylasePRO_0000149980Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei105 – 1051N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi84588.SYNW2359.

Structurei

3D structure databases

ProteinModelPortaliQ7U3S0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni287 – 29711Substrate-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.

Q7U3S0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQVADSEGWS IQDSAALYGL DRWGEPYFTI NGRGHISVQP QGERGGSLDL
60 70 80 90 100
VELVSELRGR NLGLPLLIRF DDILEDRLER LHAAFERAIA QYSYTGRYQG
110 120 130 140 150
VFPVKCNQQR HVVEELVICG KRWNFGLEAG SKAELLIALS LLDDPEALLI
160 170 180 190 200
CNGYKDRLYI ETAILARRLG RQPVVVIEQP DEVDRIIEAS KSLGAAPYIG
210 220 230 240 250
VRAKLSSRST GRWGSSVGDK AKFGLSIPEL LATVERLRES NLLPDLRLLH
260 270 280 290 300
FHIGSQINDI AVLKDALQEA GQIYVELTRL GAPMGFLDVG GGLGIDYDGS
310 320 330 340 350
RTASAASTNY SLQNYANDVV ATVRECCEPN AVAVPTLVSE SGRAIASHFS
360 370 380 390 400
LLVFDVLGSS ALSASIPNAS GDEPLTVRNL RDTLVTIQEL SGTADAQLVR
410 420 430 440 450
LQEAWNDALK FKQDALAAFR LGYMGLPDRA SAEQLTWACA DAIAQRLPKE
460 470 480 490 500
QAIPEELAAL SKALAGTYYA NLSIFRSAPD TWAIDQLFPV VPIQKLNQRP
510 520 530 540 550
TRLANLADLT CDSDGRLDRF IGDGQPKQLL ELHELDDNNP YLIGLFLSGA
560 570 580 590 600
YQEVMGNLHN LFGTTNAVHI RLSPGGSYRI DHVVRGDTNA DVLEAMEHDP
610 620 630 640
RVLLERLRVA AEAAINDGQL RIDESRRLLD HLESSLRQTT YLQD
Length:644
Mass (Da):70,760
Last modified:October 1, 2003 - v1
Checksum:iFAAF6AE897BA61EC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX569695 Genomic DNA. Translation: CAE08874.1.
RefSeqiNP_898448.1. NC_005070.1.
WP_011129212.1. NC_005070.1.

Genome annotation databases

KEGGisyw:SYNW2359.
PATRICi23836480. VBISynSp27240_2510.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX569695 Genomic DNA. Translation: CAE08874.1.
RefSeqiNP_898448.1. NC_005070.1.
WP_011129212.1. NC_005070.1.

3D structure databases

ProteinModelPortaliQ7U3S0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi84588.SYNW2359.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGisyw:SYNW2359.
PATRICi23836480. VBISynSp27240_2510.

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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: WH8102.

Entry informationi

Entry nameiSPEA_SYNPX
AccessioniPrimary (citable) accession number: Q7U3S0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: October 1, 2003
Last modified: April 1, 2015
This is version 71 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. 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.