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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Proteus mirabilis (strain HI4320)
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

Pathway: 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

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Polyamine biosynthesis, Putrescine biosynthesis, Spermidine biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

BioCyciPMIR529507:GJIW-2130-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:PMI2094
OrganismiProteus mirabilis (strain HI4320)
Taxonomic identifieri529507 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus
ProteomesiUP000008319 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 635635Biosynthetic arginine decarboxylasePRO_1000145597Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei103 – 1031N6-(pyridoxal phosphate)lysineUniRule annotation

Proteomic databases

PRIDEiB4F1A4.

Interactioni

Protein-protein interaction databases

STRINGi529507.PMI2094.

Structurei

3D structure databases

ProteinModelPortaliB4F1A4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni283 – 29311Substrate-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]
PANTHERiPTHR11482:SF36. PTHR11482:SF36. 1 hit.
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.

B4F1A4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNDNIARKMQ QTYNITYWGG GYYCANNRGN ISVCPNPDVP EATLDLTELV
60 70 80 90 100
KQVQEEHSHL RLPALFCFPQ ILQHRLRSIN AAFHRARESY GYKGDYFLVY
110 120 130 140 150
PIKVNQQRRV IESLINAGEP LGLEAGSKAE LMAVLAHANM TSSVIVCNGY
160 170 180 190 200
KDREYIRLAL TGEKLGHKVF LVIEKMSEIK MVLEEAERLE VIPRLGVRAR
210 220 230 240 250
LASQGSGKWQ ASGGEKSKFG LAATQVLQLI DTLRQAGRLD SLQLLHFHLG
260 270 280 290 300
SQMANIRDIA TGVRESARFY VELHKLGVNI QYFDVGGGLG VDYEGTRSQS
310 320 330 340 350
DCSVNYGLNE YANNVIWAIG DACDENELPH PTVITESGRA LTAHHTVLIS
360 370 380 390 400
NVIGVERNEF TAITPPAEDA PRPIASLWET WEEMQTKGNS RSLREWLHDS
410 420 430 440 450
QLDLHDVHTQ YVHGMLSLTE RAWAEELYLN ICRHIQYDLD PSNRAHRPII
460 470 480 490 500
DELQERMSDK FYVNFSLFQS LPDAWGIDQL FPVLPIEGLD KPLDRRAVLL
510 520 530 540 550
DITCDSDGII DHYVDGDGVE TTMPMPAYDP EYPPMIGFFM VGAYQEILGN
560 570 580 590 600
MHNLFGDTAA VDVYLDEKGN LTYQLSEEGD TVADMLQYVK LNPAVLLERF
610 620 630
RTQVKNAQLD KALQEQFLTE FESGLYGYTY LEEEE
Length:635
Mass (Da):71,775
Last modified:September 23, 2008 - v1
Checksum:i3EA47042A44DCA3C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM942759 Genomic DNA. Translation: CAR44185.1.
RefSeqiWP_004244147.1. NC_010554.1.
YP_002151813.1. NC_010554.1.

Genome annotation databases

EnsemblBacteriaiCAR44185; CAR44185; PMI2094.
GeneIDi6803159.
KEGGipmr:PMI2094.
PATRICi20518867. VBIProMir120933_2043.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM942759 Genomic DNA. Translation: CAR44185.1.
RefSeqiWP_004244147.1. NC_010554.1.
YP_002151813.1. NC_010554.1.

3D structure databases

ProteinModelPortaliB4F1A4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi529507.PMI2094.

Proteomic databases

PRIDEiB4F1A4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAR44185; CAR44185; PMI2094.
GeneIDi6803159.
KEGGipmr:PMI2094.
PATRICi20518867. VBIProMir120933_2043.

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
KOiK01585.
OMAiIDHYVDG.
OrthoDBiEOG676Z0R.

Enzyme and pathway databases

UniPathwayiUPA00186; UER00284.
BioCyciPMIR529507:GJIW-2130-MONOMER.

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]
PANTHERiPTHR11482:SF36. PTHR11482:SF36. 1 hit.
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: HI4320.

Entry informationi

Entry nameiSPEA_PROMH
AccessioniPrimary (citable) accession number: B4F1A4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: June 24, 2015
This is version 48 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.