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A5F0H0 (A5F0H0_VIBC3) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Biosynthetic arginine decarboxylase HAMAP-Rule MF_01417

Short name=ADC HAMAP-Rule MF_01417
EC=4.1.1.19 HAMAP-Rule MF_01417
Gene names
Name:speA HAMAP-Rule MF_01417 EMBL ABQ19043.1
Ordered Locus Names:VC0395_0419 EMBL ABQ19043.1, VC395_A0839 EMBL ACP11672.1
OrganismVibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395) [Complete proteome] [HAMAP] EMBL ABQ19043.1
Taxonomic identifier345073 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length661 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the biosynthesis of agmatine from arginine By similarity. HAMAP-Rule MF_01417

Catalytic activity

L-arginine = agmatine + CO2. SAAS SAAS002985 RuleBase RU003740 HAMAP-Rule MF_01417

Cofactor

Magnesium By similarity. SAAS SAAS002985 RuleBase RU003740 HAMAP-Rule MF_01417

Pyridoxal phosphate By similarity. SAAS SAAS002985 HAMAP-Rule MF_01417

Pathway

Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1. HAMAP-Rule MF_01417

Sequence similarities

Belongs to the Orn/Lys/Arg decarboxylase class-II family. SpeA subfamily. HAMAP-Rule MF_01417

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region311 – 32111Substrate-binding By similarity HAMAP-Rule MF_01417

Amino acid modifications

Modified residue1261N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01417

Sequences

Sequence LengthMass (Da)Tools
A5F0H0 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 44F4E37A2D81AC43

FASTA66174,465
        10         20         30         40         50         60 
MTSRVSGVIS TDEIIVILSV FVRYDVEQPS KLDRVRADYN VHYWSQGFFG IDDQGEVYVS 

        70         80         90        100        110        120 
PRKDKAHQTQ LSSIVKQLEA RDLNLPVLVR FPQILHQRVH NICDAFNQAI EEYDYPNKYL 

       130        140        150        160        170        180 
LVYPIKVNQQ KEVVDEILAS QAELEHKQLG LEAGSKPELL AVLAMAQQAS SVIVCNGYKD 

       190        200        210        220        230        240 
REYIRLALIG EKLGHKVFIV LEKLSELDLV LKEAKSLGVK PRLGLRIRLA SQGAGKWQSS 

       250        260        270        280        290        300 
GGEKSKFGLA ASQVLTVINR LKAENQLEAL QLVHFHLGSQ MANIRDVRNG VNEAVRFYCE 

       310        320        330        340        350        360 
LRELGAHIDF FDVGGGLAVD YDGTRSQSSN SMNYGLHEYA RNIVSTVSDV CNLYGQPRPV 

       370        380        390        400        410        420 
IISESGRSIT AHHAVLITNV IGTEAYSPEE IPAPGADAPM LLKNMWRGFE EVQHGTDDRA 

       430        440        450        460        470        480 
LIEIYNDTQS DLSEAHSQFA TGVLNLEHRA WAEQLSLRIY HELRQKMSNK NRFHRPILDE 

       490        500        510        520        530        540 
LQERLADKFF VNFSLFQSLP DAWGIDQVFP VLPLSGLEEM NDRRAVMLDI TCDSDGAVEQ 

       550        560        570        580        590        600 
YVEGQGIEST LPVPAWTSDK PYLMGFFLVG AYQEILGDMH NLFGDTHSAV VNINDNGESE 

       610        620        630        640        650        660 
IAFINEGDTV EDMMRYVHID VDKIRTNYRQ LVSQRVAKEE QETVLAELEL GLSGYTYLED 


F 

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References

[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 / O395 and O395 EMBL ABQ19043.1.
[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 / O395 and O395 EMBL ACP11672.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000626 Genomic DNA. Translation: ABQ19043.1.
CP001236 Genomic DNA. Translation: ACP11672.1.
RefSeqYP_001215260.1. NC_009456.1.
YP_002821908.1. NC_012583.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING345073.VC0395_0419.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ19043; ABQ19043; VC0395_0419.
ACP11672; ACP11672; VC395_A0839.
GeneID5134840.
7777902.
KEGGvco:VC0395_0419.
vcr:VC395_A0839.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1166.
HOGENOMHOG000029191.
KOK01585.
OMAMIHFHIG.
ProtClustDBPRK05354.

Enzyme and pathway databases

UniPathwayUPA00186; UER00284.

Family and domain databases

Gene3D2.40.37.10. 2 hits.
HAMAPMF_01417. SpeA.
InterProIPR009006. Ala_racemase/Decarboxylase_C.
IPR002985. Arg_decrbxlase.
IPR022643. De-COase2_C.
IPR022644. De-COase2_N.
IPR000183. Orn/DAP/Arg_de-COase.
[Graphical view]
PfamPF02784. Orn_Arg_deC_N. 1 hit.
PF00278. Orn_DAP_Arg_deC. 1 hit.
[Graphical view]
PIRSFPIRSF001336. Arg_decrbxlase. 1 hit.
PRINTSPR01180. ARGDCRBXLASE.
PR01179. ODADCRBXLASE.
TIGRFAMsTIGR01273. speA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA5F0H0_VIBC3
AccessionPrimary (citable) accession number: A5F0H0
Entry history
Integrated into UniProtKB/TrEMBL: June 12, 2007
Last sequence update: June 12, 2007
Last modified: April 16, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)