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Q116S0 (Q116S0_TRIEI) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 42. Feed History...

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

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:Tery_1142
OrganismTrichodesmium erythraeum (strain IMS101) [Complete proteome] [HAMAP] EMBL ABG50504.1
Taxonomic identifier203124 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Oscillatoriales › Trichodesmium

Protein attributes

Sequence length693 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the biosynthesis of agmatine from arginine By similarity. HAMAP MF_01417

Catalytic activity

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

Cofactor

Magnesium By similarity. HAMAP MF_01417 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

Region320 – 33011Substrate-binding By similarity HAMAP MF_01417

Amino acid modifications

Modified residue1381N6-(pyridoxal phosphate)lysine By similarity HAMAP MF_01417

Sequences

Sequence LengthMass (Da)Tools
Q116S0 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: FE5C75377432BF0C

FASTA69378,330
        10         20         30         40         50         60 
MDLHSTINEN SSQISNNTLL TNISQTDQTE INDIKSEQKK LWRIEDSEKL YKILGWGHPY 

        70         80         90        100        110        120 
FSINSVGHVT VSPKGDLGGS LDLYELVESI KQRNIGLPLI IRFSDILEDR IERLNACFSK 

       130        140        150        160        170        180 
AIARYKYKNI YRGVFPVKCN QNSHLVEEVV KFGKPHKFGL EAGSKPELLI AIATLNTTDG 

       190        200        210        220        230        240 
LIICNGYKDR EYIETAILAQ RLGKIPIIVI EQVEEVQLVI EASRKLNIKP VVGIRVKLST 

       250        260        270        280        290        300 
KGMGRWAGTT GDRAKFGLNI PEIIKVVNQL KSTGILDSLQ LLHFHIGSQI SSISVIKDAI 

       310        320        330        340        350        360 
REASQIYVEL AQLGANMKYL DVGGGLAVDY DGSKSNFYAS KNYDMQNYAN DIVAEVKEAC 

       370        380        390        400        410        420 
EEKNILPPIL ISESGRAVAS HQSVLVFDVL GVSQIPKEEP PVIGKGEHLI LQNLYETYQS 

       430        440        450        460        470        480 
INKDNYQEAY HDAIQFKEES ISIFNFGYLS ISERAKVEQL YWGCLRKIQE ILKSSEYIPN 

       490        500        510        520        530        540 
DLEELEKVMA SIYYINLSVF QSAPDSWAIN QLFPIMPIHR LDEEPTERVI LADLTCDSDG 

       550        560        570        580        590        600 
KIDRFIDLRD IKSLLELHPL QVSNKSSQYS PIQKLENSTT EIISVFEPYY LAMFLGGAYQ 

       610        620        630        640        650        660 
EIMGNLHNLF GDVNVVHIKL NPSGYKIEHV VKGDTMTEVL NYVQYNSDDL VENIRCQTEQ 

       670        680        690 
ALQEEKITLK ESRMLLQNYE SSLSSYTYLS LSN

« Hide

References

[1]"Complete sequence of Trichodesmium erythraeum IMS101."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IMS101.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000393 Genomic DNA. Translation: ABG50504.1.
RefSeqYP_720977.1. NC_008312.1.

3D structure databases

ProteinModelPortalQ116S0.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ116S0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4244412.
GenomeReviewsGene locus Tery_1142 in contig CP000393_GR.
KEGGter:Tery_1142.
NMPDRfig|203124.1.peg.3459.
PATRIC23985975. VBITriEry99848_1426.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1166.
HOGENOMHBG321436.
OMALICNGYK.
PhylomeDBQ116S0.
ProtClustDBPRK05354.

Enzyme and pathway databases

BioCycTERY203124:TERY_1142-MONOMER.

Family and domain databases

HAMAPMF_01417. SpeA.
[Tree]
InterProIPR009006. Ala_racemase/Decarboxylase_C.
IPR002985. Arg_decrbxlase.
IPR022643. De-COase2_C.
IPR022644. De-COase2_N.
IPR022653. De-COase2_pyr-phos_BS.
IPR000183. Orn/DAP/Arg_de-COase.
[Graphical view]
Gene3DG3DSA:2.40.37.10. Ala_racemase/Decarboxylase_C. 3 hits.
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.
TIGRFAMsTIGR01273. SpeA. 1 hit.
PROSITEPS00878. ODR_DC_2_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ116S0_TRIEI
AccessionPrimary (citable) accession number: Q116S0
Entry history
Integrated into UniProtKB/TrEMBL: August 22, 2006
Last sequence update: August 22, 2006
Last modified: December 14, 2011
This is version 42 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