Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q64ZT8 (SPEA_BACFR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 62. 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:BF0239
OrganismBacteroides fragilis (strain YCH46) [Complete proteome] [HAMAP]
Taxonomic identifier295405 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

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_1000024255

Regions

Region281 – 29111Substrate-binding Potential

Amino acid modifications

Modified residue991N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q64ZT8 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 9A266E486AED6C19

FASTA63071,190
        10         20         30         40         50         60 
MRKWRIEDSE ELYNITGWGT SYFGINDKGH VVVTPRKDGV AVDLKELVDE LQLRDVAAPM 

        70         80         90        100        110        120 
LVRFPDILDN RIEKTAYCFK QASEEYGYKA QNFIIYPIKV NQMRPVVEEI ISHGKKFNLG 

       130        140        150        160        170        180 
LEAGSKPELH AVIAVNTDSD SLIICNGYKD ESYIELALLA QKMGKRIFLV VEKMNELKLI 

       190        200        210        220        230        240 
ARMAKQLNVQ PNIGIRIKLA SSGSGKWEES GGDASKFGLT SSELLEALDF LESKGMKDCL 

       250        260        270        280        290        300 
KLIHFHIGSQ VTKIRRIKTA LREASQFYVQ LHAMGFNVEF VDIGGGLGVD YDGTRSSSSE 

       310        320        330        340        350        360 
SSVNYSIQEY VNDSISTLVD ASDKNGIPHP NIITESGRAL TAHHSVLIFE VLETATLPQW 

       370        380        390        400        410        420 
DDEEEIAPDA HELVQELYGI WDTLNQNKML EAWHDAQQIR EEALDLFSHG IVDLKTRAQI 

       430        440        450        460        470        480 
ERLYWSITRE INQIAGGLKH APDEFRGLSK LLADKYFCNF SLFQSLPDSW AIDQIFPIMP 

       490        500        510        520        530        540 
IQRLDEKPDR SATLQDITCD SDGKIANFIS TRNVAHYMPV HSLKQKEPYY VAVFLVGAYQ 

       550        560        570        580        590        600 
EILGDMHNLF GDTNAVHVSV NEKGYNIEQI IDGETVAEVL DYVQYSPKKL VRTLETWVTK 

       610        620        630 
SVKEGKISVE EGKEFLSNYR SGLYGYTYLE 

« Hide

References

[1]"Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation."
Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.
Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YCH46.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006841 Genomic DNA. Translation: BAD46988.1.
RefSeqYP_097522.1. NC_006347.1.

3D structure databases

ProteinModelPortalQ64ZT8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING295405.BF0239.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD46988; BAD46988; BF0239.
GeneID3081620.
KEGGbfr:BF0239.
PATRIC21046268. VBIBacFra17906_0269.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0019.
KOK01585.
OMAKPLYIGF.
OrthoDBEOG676Z0R.

Enzyme and pathway databases

UniPathwayUPA00186; UER00284.

Family and domain databases

Gene3D2.40.37.10. 2 hits.
3.20.20.10. 1 hit.
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.
IPR029066. PLP-binding_barrel.
[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.
SSF51419. SSF51419. 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_BACFR
AccessionPrimary (citable) accession number: Q64ZT8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 25, 2004
Last modified: June 11, 2014
This is version 62 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