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Protein

Biosynthetic arginine decarboxylase

Gene

speA

Organism
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Status
Unreviewed-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 annotationSAAS annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotationSAAS annotation
  • pyridoxal 5'-phosphateUniRule annotationSAAS 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

DecarboxylaseUniRule annotation, Lyase

Keywords - Biological processi

Polyamine biosynthesisUniRule annotation, Spermidine biosynthesisUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotationSAAS annotation, Metal-bindingUniRule annotation, Pyridoxal phosphateUniRule annotationSAAS annotation

Enzyme and pathway databases

UniPathwayiUPA00186; UER00284.

Names & Taxonomyi

Protein namesi
Recommended name:
Biosynthetic arginine decarboxylaseUniRule annotation (EC:4.1.1.19UniRule annotationSAAS annotation)
Short name:
ADCUniRule annotation
Gene namesi
Name:speAUniRule annotationImported
Ordered Locus Names:VC0395_0419Imported, VC395_A0839Imported
OrganismiVibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)Imported
Taxonomic identifieri345073 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000000249: Chromosome 1, UP000001630: Chromosome II

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei126 – 1261N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi345073.VC0395_0419.

Structurei

3D structure databases

ProteinModelPortaliA5F0H0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni311 – 32111Substrate-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.

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.
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.
SUPFAMiSSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR01273. speA. 1 hit.

Sequencei

Sequence statusi: Complete.

A5F0H0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSRVSGVIS TDEIIVILSV FVRYDVEQPS KLDRVRADYN VHYWSQGFFG
60 70 80 90 100
IDDQGEVYVS PRKDKAHQTQ LSSIVKQLEA RDLNLPVLVR FPQILHQRVH
110 120 130 140 150
NICDAFNQAI EEYDYPNKYL LVYPIKVNQQ KEVVDEILAS QAELEHKQLG
160 170 180 190 200
LEAGSKPELL AVLAMAQQAS SVIVCNGYKD REYIRLALIG EKLGHKVFIV
210 220 230 240 250
LEKLSELDLV LKEAKSLGVK PRLGLRIRLA SQGAGKWQSS GGEKSKFGLA
260 270 280 290 300
ASQVLTVINR LKAENQLEAL QLVHFHLGSQ MANIRDVRNG VNEAVRFYCE
310 320 330 340 350
LRELGAHIDF FDVGGGLAVD YDGTRSQSSN SMNYGLHEYA RNIVSTVSDV
360 370 380 390 400
CNLYGQPRPV IISESGRSIT AHHAVLITNV IGTEAYSPEE IPAPGADAPM
410 420 430 440 450
LLKNMWRGFE EVQHGTDDRA LIEIYNDTQS DLSEAHSQFA TGVLNLEHRA
460 470 480 490 500
WAEQLSLRIY HELRQKMSNK NRFHRPILDE LQERLADKFF VNFSLFQSLP
510 520 530 540 550
DAWGIDQVFP VLPLSGLEEM NDRRAVMLDI TCDSDGAVEQ YVEGQGIEST
560 570 580 590 600
LPVPAWTSDK PYLMGFFLVG AYQEILGDMH NLFGDTHSAV VNINDNGESE
610 620 630 640 650
IAFINEGDTV EDMMRYVHID VDKIRTNYRQ LVSQRVAKEE QETVLAELEL
660
GLSGYTYLED F
Length:661
Mass (Da):74,465
Last modified:June 12, 2007 - v1
Checksum:i44F4E37A2D81AC43
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000626 Genomic DNA. Translation: ABQ19043.1.
CP001236 Genomic DNA. Translation: ACP11672.1.
RefSeqiYP_001215260.1. NC_009456.1.
YP_002821908.1. NC_012583.1.

Genome annotation databases

EnsemblBacteriaiABQ19043; ABQ19043; VC0395_0419.
ACP11672; ACP11672; VC395_A0839.
GeneIDi5134840.
7777902.
KEGGivco:VC0395_0419.
vcr:VC395_A0839.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000626 Genomic DNA. Translation: ABQ19043.1.
CP001236 Genomic DNA. Translation: ACP11672.1.
RefSeqiYP_001215260.1. NC_009456.1.
YP_002821908.1. NC_012583.1.

3D structure databases

ProteinModelPortaliA5F0H0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi345073.VC0395_0419.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABQ19043; ABQ19043; VC0395_0419.
ACP11672; ACP11672; VC395_A0839.
GeneIDi5134840.
7777902.
KEGGivco:VC0395_0419.
vcr:VC395_A0839.

Phylogenomic databases

eggNOGiCOG1166.
HOGENOMiHOG000029191.
KOiK01585.
OMAiIDHYVDG.

Enzyme and pathway databases

UniPathwayiUPA00186; UER00284.

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.
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.
SUPFAMiSSF51419. SSF51419. 1 hit.
TIGRFAMsiTIGR01273. speA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Heidelberg J.
    Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 39541 / Classical Ogawa 395 / O395Imported and O395Imported.
  2. "A recalibrated molecular clock and independent origins for the cholera pandemic clones."
    Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.
    PLoS ONE 3:E4053-E4053(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 39541 / Classical Ogawa 395 / O395Imported and O395Imported.

Entry informationi

Entry nameiA5F0H0_VIBC3
AccessioniPrimary (citable) accession number: A5F0H0
Entry historyi
Integrated into UniProtKB/TrEMBL: June 12, 2007
Last sequence update: June 12, 2007
Last modified: March 4, 2015
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

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.