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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Pseudomonas putida (strain KT2440)
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

Enzyme and pathway databases

BioCyciPPUT160488:GIXO-585-MONOMER.

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:PP_0567
OrganismiPseudomonas putida (strain KT2440)
Taxonomic identifieri160488 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000000556 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 637637Biosynthetic arginine decarboxylasePRO_0000149972Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei110 – 1101N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi160488.PP_0567.

Structurei

3D structure databases

ProteinModelPortaliQ88QC7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni290 – 30011Substrate-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.
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.
PROSITEiPS00879. ODR_DC_2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q88QC7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVRRTRKDD GSQWTVADSR SVYGIRHWGA GYFAINEAGR VEVRPNGPQS
60 70 80 90 100
APIDLFEQVD ELRQSGLSLP LLVRFPDILQ DRVRQLTGAF DANIARLEYQ
110 120 130 140 150
SQYTALYPIK VNQQEAVVEN IIATQNVSIG LEAGSKPELL AVLALAPKGG
160 170 180 190 200
TIVCNGYKDR EFIRLALMGQ KLGHNVFIVI EKESEVALVI EEAAELKVKP
210 220 230 240 250
QVGLRVRLSS LASSKWADTG GEKSKFGLSA AQLLSVVQRF RDAGLDQGIR
260 270 280 290 300
LLHFHMGSQI ANLADYQHGF KEAIRYYGEL RALGLPVDHI DVGGGLGVDY
310 320 330 340 350
DGTHSRNASS INYDMDDYAG VVVGMLKEFC DAQGLPHPHI FSESGRSLTA
360 370 380 390 400
HHAMLVIQVT DVEKHNDDVP TIENKEALPE TVQWLVDLLG PTDIEMVTET
410 420 430 440 450
YWRATHYMGD VAAQYADGKL SLGEKALAEQ CYFAVCRRLH NSLKARQRSH
460 470 480 490 500
RQVLDELNDK LADKYICNFS VFQSLPDTWA IGQVLPIIPL HRLDEEPMRR
510 520 530 540 550
AVLQDLTCDS DGKINQYVDE QSIETSMPVH AVKEGEDYLL GVFLVGAYQE
560 570 580 590 600
ILGDMHNLFG DTDSVNIYQN ADGSVYHAGI ETHDTIEDML RYVHLSPEEL
610 620 630
MTHYRDKVAS AKITARERTQ YLDALRLGLT RSSYLSS
Length:637
Mass (Da):71,043
Last modified:June 1, 2003 - v1
Checksum:iE59F5EA60F345738
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015451 Genomic DNA. Translation: AAN66194.1.
RefSeqiNP_742730.1. NC_002947.3.

Genome annotation databases

EnsemblBacteriaiAAN66194; AAN66194; PP_0567.
GeneIDi1044357.
KEGGippu:PP_0567.
PATRICi19939209. VBIPsePut30601_0605.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015451 Genomic DNA. Translation: AAN66194.1.
RefSeqiNP_742730.1. NC_002947.3.

3D structure databases

ProteinModelPortaliQ88QC7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi160488.PP_0567.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN66194; AAN66194; PP_0567.
GeneIDi1044357.
KEGGippu:PP_0567.
PATRICi19939209. VBIPsePut30601_0605.

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
KOiK01585.
OMAiIDHYVDG.
OrthoDBiEOG676Z0R.

Enzyme and pathway databases

BioCyciPPUT160488:GIXO-585-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.
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.
PROSITEiPS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: KT2440.

Entry informationi

Entry nameiSPEA_PSEPK
AccessioniPrimary (citable) accession number: Q88QC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: June 1, 2003
Last modified: January 7, 2015
This is version 76 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.