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Q8PFQ5 (SPEA_XANAC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:XAC3923
OrganismXanthomonas axonopodis pv. citri (strain 306) [Complete proteome] [HAMAP]
Taxonomic identifier190486 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length628 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

Sequence similarities

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

Sequence caution

The sequence AAM38760.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 628628Biosynthetic arginine decarboxylase HAMAP-Rule MF_01417
PRO_0000149987

Regions

Region279 – 28911Substrate-binding Potential

Amino acid modifications

Modified residue991N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8PFQ5 [UniParc].

Last modified March 29, 2004. Version 2.
Checksum: CF03AC36E3066C05

FASTA62869,091
        10         20         30         40         50         60 
MSDWSLDQAR KTYSIPHWAD GYFDVNAAGH VVVTPTADGP AVSLPEVVDA ARAAGAKLPL 

        70         80         90        100        110        120 
LVRFPDILGQ RLGKLQAAFA QAQSEWDYAG GYTAVYPIKV NQHRGVAGTL ASHHGEGFGL 

       130        140        150        160        170        180 
EAGSKPELMA VLALSRPGGL IVCNGYKDRE YIRLALIGRK LGLQTFIVIE KPSELTLVLE 

       190        200        210        220        230        240 
EARALDVKPG LGVRMRLASL GAGKWQNSGG DKAKFGLSPR QVLDLWKTLR DTEYADSLNL 

       250        260        270        280        290        300 
LHFHMGSQIS NVRDIANGMR EATRYFVELS RLGAKISHVD VGGGLGIDYE GTRSRSYCSI 

       310        320        330        340        350        360 
NYGLHSYASN IVQPLASACE EHGLTPPRIV TECGRAMTAH HAVLIANVSE VEQAPEGRVP 

       370        380        390        400        410        420 
DAHDDEPAAI RHLREIHDEL DVRPAVELFQ EAQHFHAEGL SAYALGQIDL THRARIDDLF 

       430        440        450        460        470        480 
YAIAHGVRAR LSFDEKSHRP VLDELNERLV DKYFVNFSVF ESIPDVWAID QVFPIVPIER 

       490        500        510        520        530        540 
LNEAPQRRGI IADMTCDSDG MVKTYVENES LDSSLPLHRL NAGESYRIGF FLVGAYQEIL 

       550        560        570        580        590        600 
GDIHNLFGDT DAVEVVVDRD GYRIAQQRRG DTTDVMLDYV GYQLDTLRAT YAERIAAAHL 

       610        620 
SPERAQELSA ALEAGLTGYT YLSDEPLG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008923 Genomic DNA. Translation: AAM38760.1. Different initiation.
RefSeqNP_644224.2. NC_003919.1.

3D structure databases

ProteinModelPortalQ8PFQ5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING190486.XAC3923.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM38760; AAM38760; XAC3923.
GeneID1157994.
KEGGxac:XAC3923.
PATRIC24060012. VBIXanAxo33670_4051.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycXAXO190486:GH55-3923-MONOMER.

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.
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.
PROSITEPS00879. ODR_DC_2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSPEA_XANAC
AccessionPrimary (citable) accession number: Q8PFQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: March 29, 2004
Last modified: February 19, 2014
This is version 71 of the entry and version 2 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