Gene_locus Report for: rhofd-q21u70Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) poly-beta-hydroxybutyrate polymerase-like Relationship (Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Bacteria: N E > Proteobacteria: N E > Betaproteobacteria: N E > Burkholderiales: N E > Comamonadaceae: N E > Rhodoferax: N E > Rhodoferax ferrireducens: N E
5_AlphaBeta_hydrolase : rhofd-q21zf7Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) phospholipase/carboxylesterase precursor. 6_AlphaBeta_hydrolase : rhofd-q21tn5Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) alpha/beta hydrolase, rhofd-q21uj6Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) alpha/beta hydrolase, rhofd-q21uy8Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) alpha/beta hydrolase, rhofd-q21wq8Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) alpha/beta hydrolase, rhofd-q21xe5Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) alpha/beta hydrolase, rhofd-q222i7Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) alpha/beta hydrolase, rhofd-q222j1Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) alpha/beta hydrolase precursor, rhofd-q222t1Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) alpha/beta hydrolase precursor. A85-EsteraseD-FGH : rhofd-q223c0Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) carboxylesterase (EC 3.1.1.1). abh_upf00227 : rhofd-q21t19Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) hypothetical protein. Aclacinomycin-methylesterase_RdmC : rhofd-q21vw5Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) alpha/beta hydrolase. Bacterial_lip_FamI.1 : rhofd-q21t36Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) triacylglycerol lipase precursor (EC 3.1.1.3). Dienelactone_hydrolase : rhofd-q21ru3Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) carboxymethylenebutenolidase (EC 3.1.1.45), rhofd-q21t81Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) twin-arginine translocation pathway signal (EC 3.1.1.45). DLH-S : rhofd-q222a4Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) dienelactone hydrolase. Epoxide_hydrolase : rhofd-q21tk5Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) alpha/beta hydrolase. Homoserine_transacetylase : rhofd-q221z3Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) homoserine o-acetyltransferase (EC 2.3.1.31). Hormone-sensitive_lipase_like : rhofd-q21vs0Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) alpha/beta hydrolase fold-3 precursor, rhofd-q21vv3Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) alpha/beta hydrolase fold-3, rhofd-q21yh6Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) alpha/beta hydrolase fold-3. Hydrolase-1_PEP : rhofd-q220v8Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) esterase/lipase/thioesterase family active site. Hydrolase_RBBP9_YdeN : rhofd-q21vt2Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) hypothetical protein, rhofd-q21xl1Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) hypothetical protein, rhofd-q223l6Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) hypothetical protein. Lipase_3 : rhofd-q21ux0Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) hemolysin-type calcium-binding protein precursor, rhofd-q21ux2Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) hypothetical protein. LYsophospholipase_carboxylesterase : rhofd-q21ve9Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) phospholipase/carboxylesterase, rhofd-q21xu9Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) carboxylesterase (EC 3.1.1.1). Monoglyceridelipase_lysophospholip : rhofd-q221z7Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) alpha/beta hydrolase. OHBut_olig_hydro_put : rhoft-hbohRhodoferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118) (Albidiferax ferrireducens). D-(-)-3-hydroxybutyrate oligomer hydrolase. PGAP1 : rhofd-q21sk3Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) pgap1-like. PHA_synth_I : rhofd-q21vc4Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) poly(r)-hydroxyalkanoic acid synthase, class i. PHB_depolymerase_PhaZ : rhofd-q21vz6Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) polyhydroxyalkanoate depolymerase, intracellular. Proline_iminopeptidase : rhofd-q223f3Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) proline iminopeptidase (EC 3.4.11.5). Xaa-Pro-like_dom : rhofd-q222h6Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) alpha/beta hydrolase Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)Rhodoferax ferrireducens DSM 15236: N, E.
Rhodoferax ferrireducens T118: N, E.
Molecular evidence | | Database | No mutation
No structure
No kinetic
No Substrate
No inhibitor
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Sequence Graphical view for this peptide sequence: rhofd-q21u70
Colored MSA for PhaC_cen_dom (raw)
MKKSIPLPPPTERQLAAAQALDEAFHSQLAKVNLGLSPISLALAYADWAM
HLATSPGQQMLLAQRALALSQQALSSPWQEQLASDDASQPAPVDDPRFSD
PGWRHWPFNVLKESFKATSSWWHEASQVEGVSSHHRHVVDFFNRQGLDAL
SPSNLPVTNPEAIKKGKESLGQSWLKGYQHLALDLLERSQHTGGASRTAL
KPLPFKVGQDVAVTPGKVVFRNHLIELIQYTPTTAGVYPEPLLIVPSCIM
KYYILDLSPGNSMVRYLVGQGHTVFMISWRNPDASDRELGMQDYLQLGVM
EAMAAVKSLTGAPRIHALGYCLGGTFLAIVAAALGARQPQSHRRGQGKNQ
HRRREDAVALDTMPELASVTLLAAQTDFSEPGELGVFIDDDQLKTLRESM
ARTGYLSGRQMAGSFQFLNSRDLVWSRNTRRYLLGQDEVGNDMMSWNADV
TRLPERMHNEYLSSLFLNNALATGNYRVAGVGVALMDIRAPLLVVGTQRD
HVSPWQSVYKIHLLTDTQTTFILAAGGHNAGIVSEPGHRGRSYQMDCMEK
GHAWTEPDDWAAHAPLFEGSWWEAMHRWLQERSGKPVPPPAINPATVLGD
APGDYVMARYAD
Legend
This sequence has been compared to family alignement (MSA)
red => minority aminoacid
blue => majority aminoacid
color intensity => conservation rate
title => sequence position(MSA position)aminoacid rate
Catalytic site
Catalytic site in the MSA
MKKSIPLPPPTERQLAAAQALDEAFHSQLAKVNLGLSPISLALAYADWAM
HLATSPGQQMLLAQRALALSQQALSSPWQEQLASDDASQPAPVDDPRFSD
PGWRHWPFNVLKESFKATSSWWHEASQVEGVSSHHRHVVDFFNRQGLDAL
SPSNLPVTNPEAIKKGKESLGQSWLKGYQHLALDLLERSQHTGGASRTAL
KPLPFKVGQDVAVTPGKVVFRNHLIELIQYTPTTAGVYPEPLLIVPSCIM
KYYILDLSPGNSMVRYLVGQGHTVFMISWRNPDASDRELGMQDYLQLGVM
EAMAAVKSLTGAPRIHALGYCLGGTFLAIVAAALGARQPQSHRRGQGKNQ
HRRREDAVALDTMPELASVTLLAAQTDFSEPGELGVFIDDDQLKTLRESM
ARTGYLSGRQMAGSFQFLNSRDLVWSRNTRRYLLGQDEVGNDMMSWNADV
TRLPERMHNEYLSSLFLNNALATGNYRVAGVGVALMDIRAPLLVVGTQRD
HVSPWQSVYKIHLLTDTQTTFILAAGGHNAGIVSEPGHRGRSYQMDCMEK
GHAWTEPDDWAAHAPLFEGSWWEAMHRWLQERSGKPVPPPAINPATVLGD
APGDYVMARYAD
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