Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210)
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

BioCyciGMET269799:GHNY-912-MONOMER.
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:Gmet_0904
OrganismiGeobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210)
Taxonomic identifieri269799 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter
ProteomesiUP000007073: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 635635Biosynthetic arginine decarboxylasePRO_1000068490Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei100 – 1001N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi269799.Gmet_0904.

Structurei

3D structure databases

ProteinModelPortaliQ39X78.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni282 – 29211Substrate-bindingUniRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
KOiK01585.
OMAiMIILESL.
OrthoDBiEOG676Z0R.

Family and domain databases

Gene3Di3.20.20.10. 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.

Q39X78-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MERWSINDSA KIYNLPNWGA DLFSINKKGN VCVHPSPTSK HSIDLRALVD
60 70 80 90 100
DLIKRKIKPP ILLRFMDVLQ GRIAAINRAF KYAIDENDYP STYQTFYPIK
110 120 130 140 150
VNQQRQVVEA IAKFGKRYNI GIEVGSKPEL VIGISFATGN GIPIICNGYK
160 170 180 190 200
DKEYIETVLY ATKIGYDITI VVEKMFELEK IIALSKKTGI KPKLGIRVKL
210 220 230 240 250
SSKGTGKWAT SGGEDAKFGL RMSEIIAAIG LLEQNELLDS VKLIHFHIGS
260 270 280 290 300
QITKIDKIKS ALIEGTRVYA EMRKLGVGIE YVDIGGGLGV DYDGSKSSYF
310 320 330 340 350
SSVNYSIEEY ANDVIYQIKN ICEDAGVECP NIISESGRAT AAHYSVLVTN
360 370 380 390 400
LLNTNTQNLM PDFEETLNGA EKLAPTVKKL VDIYKSIDRY SLREDYHDTV
410 420 430 440 450
QLIQEAVSLF SLGYLTLAER AMAEWLHGKI LRKINGIVEK IKPIPEELQN
460 470 480 490 500
FQLSLRQTYF ANFSLFQSIP DSWAIDQLFP IVPIQRLNQK PDVMASIADI
510 520 530 540 550
TCDSDGEITS FVGENGRTKY LPLHKIRKDE DYFVGFFLIG AYQEILGDMH
560 570 580 590 600
NLFGDTNAVH VTFNKKTGYK IDTVINGDAT WESLKYVQYK GPEILKHVRD
610 620 630
TMEKDVALRK VSIEESSHFL ELLDRTLLGY TYLGE
Length:635
Mass (Da):71,521
Last modified:November 22, 2005 - v1
Checksum:i689186DAE924266B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000148 Genomic DNA. Translation: ABB31146.1.
RefSeqiYP_006719870.1. NC_007517.1.

Genome annotation databases

EnsemblBacteriaiABB31146; ABB31146; Gmet_0904.
GeneIDi3738242.
KEGGigme:Gmet_0904.
PATRICi22000996. VBIGeoMet55070_0939.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000148 Genomic DNA. Translation: ABB31146.1.
RefSeqiYP_006719870.1. NC_007517.1.

3D structure databases

ProteinModelPortaliQ39X78.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi269799.Gmet_0904.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABB31146; ABB31146; Gmet_0904.
GeneIDi3738242.
KEGGigme:Gmet_0904.
PATRICi22000996. VBIGeoMet55070_0939.

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
KOiK01585.
OMAiMIILESL.
OrthoDBiEOG676Z0R.

Enzyme and pathway databases

UniPathwayiUPA00186; UER00284.
BioCyciGMET269799:GHNY-912-MONOMER.

Family and domain databases

Gene3Di3.20.20.10. 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. "Complete sequence of Geobacter metallireducens GS-15."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
    Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: GS-15 / ATCC 53774 / DSM 7210.

Entry informationi

Entry nameiSPEA_GEOMG
AccessioniPrimary (citable) accession number: Q39X78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 22, 2005
Last modified: February 4, 2015
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, 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.