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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Rhodopirellula baltica (strain SH1)
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:RB3708
OrganismiRhodopirellula baltica (strain SH1)
Taxonomic identifieri243090 [NCBI]
Taxonomic lineageiBacteriaPlanctomycetesPlanctomycetiaPlanctomycetalesPlanctomycetaceaeRhodopirellula
ProteomesiUP000001025 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 668668Biosynthetic arginine decarboxylasePRO_0000149974Add
BLAST

Amino acid modifications

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

Interactioni

Protein-protein interaction databases

STRINGi243090.RB3708.

Structurei

3D structure databases

ProteinModelPortaliQ7UTS2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni286 – 29611Substrate-bindingUniRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
InParanoidiQ7UTS2.
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.
PROSITEiPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7UTS2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSVLDSKWT RSDASKTYDI DRWGAGYFSI SDAGTVLVSP DRDPSQSIDL
60 70 80 90 100
KELVDRLGQR NLDLPILLRF NGILRDRLRE LDRCFKNAIH DHKYQSRYRC
110 120 130 140 150
VFPIKVNQQR EVVQQIVSEG ARLGFGIEAG SKPELVAAVA MGDANVPIVC
160 170 180 190 200
NGFKDEEFIR LALLAQRLGR NVLPVVEKVS ELDLILDVAK DIGVRPTIGM
210 220 230 240 250
RVKLATRGSG RWQASGGYRS KFGLTVAELL AQLDRLIAMD MGDCLQLLHF
260 270 280 290 300
HVGSQIGNIR QLKSAILEAA RIYVDLVRRG AGMRYLDVGG GLGVDYDGSR
310 320 330 340 350
SDSESSMNYT MQEYANDVVY HTQTVCDEAG VPHPELISES GRAVAAHHSV
360 370 380 390 400
LVMETLGVTS QGVANLPCWA KVEGEPVSPD HGGIEMDSVG AIETSEMEGP
410 420 430 440 450
PESYEQPVHD LWVGYVNMTQ ANMMETFHDA QVALDLCMNL FSGGYLPLEQ
460 470 480 490 500
RVAAENLYFA ICHRVRELAE SMKERPDDLK HLDRMLSDIY FANFSLFQSM
510 520 530 540 550
PDSWAIDQLF PIMPIHRLLE KPSRHAVLGD ITCDSDGKVD AFVCGGGRQR
560 570 580 590 600
TLMLHPLKSG EPYQLAVFMV GAYQEILGDL HNLFGDTHAV HVDIEDGVTK
610 620 630 640 650
VRSIVKGDTV SEVLGYVQYE DRELIENLQE SVESAIGNGH IDHQQAGETV
660
AAYERALSGY TYLSTRTK
Length:668
Mass (Da):74,081
Last modified:September 30, 2003 - v1
Checksum:i3851560B071E60A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX294139 Genomic DNA. Translation: CAD73363.1.
RefSeqiNP_865678.1. NC_005027.1.

Genome annotation databases

GeneIDi1797121.
KEGGirba:RB3708.
PATRICi23244879. VBIRhoBal59814_1723.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX294139 Genomic DNA. Translation: CAD73363.1.
RefSeqiNP_865678.1. NC_005027.1.

3D structure databases

ProteinModelPortaliQ7UTS2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243090.RB3708.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1797121.
KEGGirba:RB3708.
PATRICi23244879. VBIRhoBal59814_1723.

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
InParanoidiQ7UTS2.
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.
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: SH1.

Entry informationi

Entry nameiSPEA_RHOBA
AccessioniPrimary (citable) accession number: Q7UTS2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 28, 2004
Last sequence update: September 30, 2003
Last modified: March 31, 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.