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Q9K9K5 (SPEA_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 74. 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:
Arginine decarboxylase

EC=4.1.1.19
Gene names
Name:speA
Ordered Locus Names:BH2640
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the formation of agmatine from arginine By similarity.

Catalytic activity

L-arginine = agmatine + CO2.

Cofactor

Pyridoxal phosphate By similarity.

Pathway

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

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the Orn/Lys/Arg decarboxylase class-I family.

Ontologies

Keywords
   Biological processPolyamine biosynthesis
Putrescine biosynthesis
Spermidine biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionDecarboxylase
Lyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processputrescine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

spermidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionarginine decarboxylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 491491Arginine decarboxylase
PRO_0000201146

Amino acid modifications

Modified residue2271N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9K9K5 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 3C2ACC55C3C57F5D

FASTA49153,449
        10         20         30         40         50         60 
MSRQEQTPLF SGVVAHAKHN PVQFHIPGHK KGAGMDPAFR SFIGDNALSI DLINIGPLDD 

        70         80         90        100        110        120 
LHHPHGIIKE AQELAAEAFG ADHTFFSVQG TSGAIMTMIM SVVGPGEKII VPRNVHKSIM 

       130        140        150        160        170        180 
SAIVFSGATP VFIHPEIDPL LGISHGITIE AVEKALDAHP DAKGLLVINP TYFGIAANLK 

       190        200        210        220        230        240 
KIVELCHSRD VPVLVDEAHG VHIHFHEALP LSAMQAGADM AATSVHKLGG SLTQSSILNV 

       250        260        270        280        290        300 
REGLVSAKRV QTIISMLTTT STSYLLLASL DAARKHLATN GRDLIGYTIQ LADQARDQIN 

       310        320        330        340        350        360 
AIDGLYCVGK EILGTIATYD YDPTKLIISV KNLGITGYDA EVWLREHYQI EVELSDLYNI 

       370        380        390        400        410        420 
LCIVSFGDTE REMDLLVKAL SELADLHKHG ICERSPVSVY VPNIPTLAMS PRDAFYAETE 

       430        440        450        460        470        480 
VVPFEDSVGR TIAEFIMVYP PGIPILIPGE IITESNLAYI RENNRAGLPV QGPEDDTFRT 

       490 
LRVIKEHEAI R 

« Hide

References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000004 Genomic DNA. Translation: BAB06359.1.
PIRH83979.
RefSeqNP_243506.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9K9K5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272558.BH2640.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB06359; BAB06359; BAB06359.
GeneID892594.
KEGGbha:BH2640.
PATRIC18942470. VBIBacHal18977_2748.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1982.
HOGENOMHOG000083489.
KOK01582.
OMAMYNILCL.
OrthoDBEOG61CKX5.
ProtClustDBCLSK873379.

Enzyme and pathway databases

BioCycBHAL272558:GJC5-2724-MONOMER.
UniPathwayUPA00186; UER00284.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.100.10. 1 hit.
InterProIPR000310. Orn/Lys/Arg_deCO2ase_major_dom.
IPR008286. Prn/Lys/Arg_de-COase_C.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PfamPF01276. OKR_DC_1. 1 hit.
PF03711. OKR_DC_1_C. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
SSF55904. SSF55904. 1 hit.
PROSITEPS00703. OKR_DC_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSPEA_BACHD
AccessionPrimary (citable) accession number: Q9K9K5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: October 1, 2000
Last modified: November 13, 2013
This is version 74 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