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Q9JT25 (SPEA_NEIMA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Biosynthetic arginine decarboxylase

Short name=ADC
EC=4.1.1.19
Gene names
Name:speA
Ordered Locus Names:NMA2017
OrganismNeisseria meningitidis serogroup A / serotype 4A (strain Z2491) [Complete proteome] [HAMAP]
Taxonomic identifier122587 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length630 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. HAMAP-Rule MF_01417

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01417

Pyridoxal phosphate By similarity. 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 630630Biosynthetic arginine decarboxylase HAMAP-Rule MF_01417
PRO_0000149964

Regions

Region279 – 28911Substrate-binding Potential

Amino acid modifications

Modified residue991N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9JT25 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 1E33ACEE7929F314

FASTA63070,901
        10         20         30         40         50         60 
MPILTIREVC NINHWGIGYY DVDDSGEIIV RPNPSQHNQI VSLQKLTEAV QQKHQARLPV 

        70         80         90        100        110        120 
LFCFPQILEH RLRDINRAFQ TAREECGYKG GYCLVYPIKV NQHRRVIESL MSSGQPHGLE 

       130        140        150        160        170        180 
AGSKAELMAV LAHAGTRQTL IVCNGYKDRE YIRFALMGEK LGHQVYLVIE KLSEIQMVLE 

       190        200        210        220        230        240 
EAEKLGIKPR LGVRARLASQ GSGKWQSSGG EKSKFGLSAS QVLQLVDILK QKNRLDCLQL 

       250        260        270        280        290        300 
LHFHLGSQLG NIRDVATGVH ESARFYVELH KLGVNIRCFD VGGGLGVDYE GNRTQSDCSV 

       310        320        330        340        350        360 
NYSLNEYAAT VVWGISQACL EHGLPHPTII TESGRGITAH HAVLVANVIG VERYKPRRLD 

       370        380        390        400        410        420 
APSPEAPRVL HSMWETWTDI SASREKRSLR SWIHEGQFDL ADVHNQYNVG LLSLAQRAWA 

       430        440        450        460        470        480 
EQLYLNICHE VGELFNEKHR SHRTIIDELQ ERFADKLYVN FSLFQSLPDA WGIDQLFPVC 

       490        500        510        520        530        540 
PITGLNEPIA RRAVLLDITC DSDGTIDHYI DGDGIAGTMP MPDYPEEEPP LLGFFMVGAY 

       550        560        570        580        590        600 
QEILGNMHNL FGDTATADVV VGEDGQFTVI DYDEGNTVAD MLEYVYQDPK ELMKRYREQI 

       610        620        630 
EHSDLPASQA MSFLKELEAG LNGYTYLEDE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL157959 Genomic DNA. Translation: CAM09122.1.
PIRD81831.
RefSeqYP_002343280.1. NC_003116.1.

3D structure databases

ProteinModelPortalQ9JT25.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING122587.NMA2017.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM09122; CAM09122; NMA2017.
GeneID907423.
KEGGnma:NMA2017.
PATRIC20365426. VBINeiMen132687_2399.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1166.
HOGENOMHOG000029191.
KOK01585.
OMAMIHFHIG.
OrthoDBEOG676Z0R.
ProtClustDBPRK05354.

Enzyme and pathway databases

BioCycNMEN122587:GI3Q-1855-MONOMER.
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.
IPR022657. De-COase2_CS.
IPR022644. De-COase2_N.
IPR022653. De-COase2_pyr-phos_BS.
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.
SUPFAMSSF50621. SSF50621. 1 hit.
TIGRFAMsTIGR01273. speA. 1 hit.
PROSITEPS00878. ODR_DC_2_1. 1 hit.
PS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSPEA_NEIMA
AccessionPrimary (citable) accession number: Q9JT25
Secondary accession number(s): A1ITK5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways