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 sp. (strain M21)
Status
Reviewed-Annotation score: -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: agmatine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes agmatine from L-arginine.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Biosynthetic arginine decarboxylase (speA)
This subpathway is part of the pathway agmatine biosynthesis, which is itself part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes agmatine from L-arginine, the pathway agmatine biosynthesis and in Amine and polyamine biosynthesis.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDecarboxylase, Lyase
Biological processPolyamine biosynthesis, Spermidine biosynthesis
LigandMagnesium, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

BioCyciGSP443144:G1GFA-1326-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:GM21_1309
OrganismiGeobacter sp. (strain M21)
Taxonomic identifieri443144 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter
Proteomesi

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10002152471 – 635Biosynthetic arginine decarboxylaseAdd BLAST635

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei100N6-(pyridoxal phosphate)lysineUniRule annotation1

Proteomic databases

PRIDEiC6E3V4

Interactioni

Protein-protein interaction databases

STRINGi443144.GM21_1309

Structurei

3D structure databases

ProteinModelPortaliC6E3V4
SMRiC6E3V4
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni282 – 292Substrate-bindingUniRule annotationAdd BLAST11

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105DP5 Bacteria
COG1166 LUCA
HOGENOMiHOG000029191
KOiK01585
OMAiLFPIMPI
OrthoDBiPOG091H04NG

Family and domain databases

CDDicd06830 PLPDE_III_ADC, 1 hit
Gene3Di2.40.37.10, 3 hits
3.20.20.10, 1 hit
HAMAPiMF_01417 SpeA, 1 hit
InterProiView protein in InterPro
IPR009006 Ala_racemase/Decarboxylase_C
IPR002985 Arg_decrbxlase
IPR022657 De-COase2_CS
IPR022644 De-COase2_N
IPR022653 De-COase2_pyr-phos_BS
IPR000183 Orn/DAP/Arg_de-COase
IPR029066 PLP-binding_barrel
PANTHERiPTHR43295 PTHR43295, 1 hit
PfamiView protein in Pfam
PF02784 Orn_Arg_deC_N, 1 hit
PIRSFiPIRSF001336 Arg_decrbxlase, 1 hit
PRINTSiPR01180 ARGDCRBXLASE
PR01179 ODADCRBXLASE
SUPFAMiSSF50621 SSF50621, 1 hit
SSF51419 SSF51419, 1 hit
TIGRFAMsiTIGR01273 speA, 1 hit
PROSITEiView protein in PROSITE
PS00878 ODR_DC_2_1, 1 hit
PS00879 ODR_DC_2_2, 1 hit

Sequencei

Sequence statusi: Complete.

C6E3V4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKWTINDSS KIYNIDNWGA ELFSINKKGN VCVHPSPNSK YSIDLKVLVD
60 70 80 90 100
DLIKRKIKPP ILLRFMNILE GRIASISRVF KNAISDNNYP AKYQTFYPIK
110 120 130 140 150
VNQQRQVVEA IANFGKKYNI GLEVGSKPEL VAAISMSTGN NLPILCNGYK
160 170 180 190 200
DTEFIETVLF ATRVGYDITI VVEKLFELEK IVEVSKRTGI VPKLGIRVKL
210 220 230 240 250
SSKGIGKWST SGGDDAKFGL RISELIAAIE MLKQNDMLDS VKLLHFHVGS
260 270 280 290 300
QITKIDKIKN ALIEGTRIYA EMRKLGVNLE FLDIGGGLGV DYDGSKSSYF
310 320 330 340 350
SSVNYSLEEY ANDVIYQVKN ICDDAGVPCP NIISESGRAT VAHYSVLVTD
360 370 380 390 400
VLNNNTQTLM PDFESILTES EKLSPTVKKL VDIYKSIDKH SLREDYHDTI
410 420 430 440 450
QLIQESVSLF NLGYLNMAER ANAEWICSKI IRKINSIVEK MKPIPDELQN
460 470 480 490 500
FQLSLRQTYF ANFSLFQSIP DSWAIDQLFP IVPIQRLDEK PDVLTSIADI
510 520 530 540 550
TCDSDGEITS FVGENGRTKA LPLHKIKVDE QYYIGFFLIG AYQEILGDMH
560 570 580 590 600
NLFGDTNAVH ITFNKKTNYK IDTVITGDAT WESLKYVQYD SQEILKRVRN
610 620 630
NLEKDVSLQK VSIEESSHFL ELLDKTLQSY TYLGE
Length:635
Mass (Da):71,705
Last modified:September 1, 2009 - v1
Checksum:i588FE255ED8B7EB4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001661 Genomic DNA Translation: ACT17369.1
RefSeqiWP_015836621.1, NC_012918.1

Genome annotation databases

EnsemblBacteriaiACT17369; ACT17369; GM21_1309
KEGGigem:GM21_1309

Similar proteinsi

Entry informationi

Entry nameiSPEA_GEOSM
AccessioniPrimary (citable) accession number: C6E3V4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 1, 2009
Last modified: May 23, 2018
This is version 51 of the entry and version 1 of the sequence. See 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

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health