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B6YQA1 (B6YQA1_AZOPC) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 23. 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 MF_01417
Short name=ADC HAMAP MF_01417
EC=4.1.1.19 HAMAP MF_01417
Gene names
Name:speA HAMAP MF_01417
Ordered Locus Names:CFPG_110
OrganismAzobacteroides pseudotrichonymphae genomovar. CFP2 [Complete proteome] [HAMAP]
Taxonomic identifier511995 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Candidatus Azobacteroides

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 MF_01417 SAAS SAAS009006

Catalytic activity

L-arginine = agmatine + CO2. HAMAP MF_01417 SAAS SAAS009006 RuleBase RU003740

Cofactor

Magnesium By similarity. HAMAP MF_01417 RuleBase RU003740 SAAS SAAS009006

Pyridoxal phosphate By similarity. HAMAP MF_01417 SAAS SAAS000183

Pathway

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

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region281 – 29111Substrate-binding By similarity HAMAP MF_01417

Amino acid modifications

Modified residue991N6-(pyridoxal phosphate)lysine By similarity HAMAP MF_01417

Sequences

Sequence LengthMass (Da)Tools
B6YQA1 [UniParc].

Last modified January 20, 2009. Version 1.
Checksum: 986CB13CDC55CD94

FASTA63072,195
        10         20         30         40         50         60 
MRKWRIEDSM ELYNIHGWGL GYFSVNDKGH IIVSPKKDCA VVDLKELIDE LTLRDVDAPL 

        70         80         90        100        110        120 
LVRFPDILDN RIEKISGCFK TSAKEYNYTA QNFIIYPIKV NQMRQVVEEI VNHGKKFNIG 

       130        140        150        160        170        180 
LEAGSKPELH AVLAINTCSD SLIVCNGYKD ENYIRLALLA QKMGKNIFIV VEKLNELKLI 

       190        200        210        220        230        240 
AELAKKVKIY PNIGIRIKLA SSGSGKWEES GGDGSKFGLS SSELLEAIDF MNKNKLKDCL 

       250        260        270        280        290        300 
KLIHFHIGSQ VTKIRRIKNA LREASQFYVQ LRSIGYEIEF VDIGGGLGVD YDGTRNDRSE 

       310        320        330        340        350        360 
SSMNYSIQEY VNDSISTLVD VCMKNSIPQP NIITECGRSL TAHHSVLIFQ VLETAILPEW 

       370        380        390        400        410        420 
KEDEKLPKNT HELVQELYKL WDEMNHPRLI ETWHDAQQIR EESLNLFSLG MLDLTTRAQI 

       430        440        450        460        470        480 
EKLYWSIARE VQQMTLNMKH APEELRKVSR ILPDKYFCNF SLFRSLPDSW AIDQVFPIVP 

       490        500        510        520        530        540 
IDRLGEKPSR TATLQDMTCD SDGKIDNFIN MKLSTYHLPV HPISKKDSYY IGVFLVGAYQ 

       550        560        570        580        590        600 
EILGDLHNLF GETNAVHVSV NKNDYQIEQI IDGERVADVL EYVQYNTKRL VRTVETWVTA 

       610        620        630 
SMKEGKITVE EGREFLSNYR SGLYGYTYLE

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References

[1]"Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT protist cells in termite gut."
Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T., Sakaki Y., Toyoda A., Hattori M., Ohkuma M.
Science 322:1108-1109(2008) [PubMed: 19008447] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP010656 Genomic DNA. Translation: BAG83373.1.
RefSeqYP_002308784.1. NC_011565.1.

3D structure databases

ProteinModelPortalB6YQA1.
ModBaseSearch...

Protein-protein interaction databases

STRINGB6YQA1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7039779.
GenomeReviewsGene locus CFPG_110 in contig AP010656_GR.
KEGGaps:CFPG_110.
PATRIC31961739. VBICanAzo57536_0254.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG321436.
OMALICNGYK.
ProtClustDBPRK05354.

Family and domain databases

HAMAPMF_01417. SpeA.
[Tree]
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]
KOK01585.
PANTHERPTHR11482:SF3. Arg_decrbxlase. 1 hit.
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. Racem_decarbox_C. 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 nameB6YQA1_AZOPC
AccessionPrimary (citable) accession number: B6YQA1
Entry history
Integrated into UniProtKB/TrEMBL: January 20, 2009
Last sequence update: January 20, 2009
Last modified: December 14, 2011
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info