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Q7TUJ9 (SPEA_PROMM) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Biosynthetic arginine decarboxylase

Short name=ADC
EC=4.1.1.19
Gene names
Name:speA
Ordered Locus Names:PMT_2150
OrganismProchlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]
Taxonomic identifier74547 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length648 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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 648648Biosynthetic arginine decarboxylase HAMAP-Rule MF_01417
PRO_0000149969

Regions

Region291 – 30111Substrate-binding Potential

Amino acid modifications

Modified residue1091N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7TUJ9 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: BBFEE45E4F8E395B

FASTA64871,364
        10         20         30         40         50         60 
MSAADPIQDN KSWTVADSAA LYGLDHWGHP YFSANANGHV QVQPRGDQGS CLDLVELVEE 

        70         80         90        100        110        120 
LKSRNLNLPL LIRFDDILED RLERLHSAFE EAISKYGYAG RYQGVFPVKC NQQRHVVEQL 

       130        140        150        160        170        180 
VESGRQWHFG LEAGSKAELL IALSLVNDPE ALLICNGYKD QRYIETAILA RRLGRQPVVV 

       190        200        210        220        230        240 
IEQPDEVERI IRSSQELGAA PFLGVRAKLT TRSTGHWSSS VGEKAKFGLS VPDLLATVEA 

       250        260        270        280        290        300 
LRQADLLSDL RLLHFHIGSQ INDIAVLKDA LQEAAQIYVE LTKLGAPMGY LDVGGGLGVD 

       310        320        330        340        350        360 
YDGSRSASAA STNYSLQNYA NDVVATVREC CKPHGITLPI LVSESGRAIA SHFSILVFDV 

       370        380        390        400        410        420 
LGTGTVPGAI PKQTVEEPLT IHNLRETLSG VMATQKGAVS EISRLQEAWN DAIKFKEDAL 

       430        440        450        460        470        480 
AAFRLGYISL PERALAEQLT GACAEAIMGQ LPCNETIPDD LQSLRAVLAS TYYANLSIFR 

       490        500        510        520        530        540 
SAPDTWAIEQ LFPLMPIHRL NEEPTQLGHF ADLTCDSDGK LDRFIGNGQT KTLLELHNLR 

       550        560        570        580        590        600 
QNEAYMIGMF LAGAYQEVMG NLHNLFGSTN AVHIRLTTAG GYQVDHVVRG NTNSEVLEAM 

       610        620        630        640 
EHNPELLLER LRLASELAIQ RGELKINDVR RLMDHLEASL RQTTYLQG 

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9313.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548175 Genomic DNA. Translation: CAE22324.1.
RefSeqNP_895974.1. NC_005071.1.

3D structure databases

ProteinModelPortalQ7TUJ9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING74547.PMT2150.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE22324; CAE22324; PMT_2150.
GeneID1727896.
KEGGpmt:PMT2150.
PATRIC23013213. VBIProMar135351_2729.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1166.
KOK01585.
OMAIDHYVDG.
OrthoDBEOG676Z0R.

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_PROMM
AccessionPrimary (citable) accession number: Q7TUJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: October 1, 2003
Last modified: June 11, 2014
This is version 67 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