Gene_locus Report for: pardp-a1b0m3

Paracoccus denitrificans (strain Pd 1222) putative uncharacterized protein

Relationship

Family	\|	AlphaBeta_hydrolase
Block	\|	X
Position in NCBI Life Tree	\|	Paracoccus denitrificans

(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 > Alphaproteobacteria: N E > Rhodobacterales: N E > Rhodobacteraceae: N E > Paracoccus: N E > Paracoccus denitrificans: N E

There are 28 a/b hydrolases in Paracoccus denitrificans view in a: Table

6_AlphaBeta_hydrolase : pardp-a1b0v9Paracoccus denitrificans (strain Pd 1222) Alpha/beta hydrolase fold protein, pardp-a1b2k5Paracoccus denitrificans (strain Pd 1222) 3-hydroxybutyrate oligomer hydrolase phaZc, pardp-a1b8p3Paracoccus denitrificans (strain Pd 1222) alpha/beta hydrolase fold, pardp-a1b737Paracoccus denitrificans (strain Pd 1222) alpha/beta hydrolase fold, pardp-a1bbt7Paracoccus denitrificans (strain Pd 1222) alpha/beta hydrolase fold.
A85-EsteraseD-FGH : parde-FGHAParacoccus denitrificans Paracoccus denitrificans PD1222 s-formylglutathione hydrolase.
A85-IroE-IroD-Fes-Yiel : pardp-a1b5g7Paracoccus denitrificans (strain Pd 1222) Putative uncharacterized protein, pardp-a1b558Paracoccus denitrificans (strain Pd 1222) Putative esterase.
ABHD11-Acetyl_transferase : pardp-a1b0i5Paracoccus denitrificans (strain Pd 1222) Alpha/beta hydrolase fold protein.
Abhydrolase_9 : pardp-a1azr2Paracoccus denitrificans (strain Pd 1222) Putative uncharacterized protein.
AcoC_BiotinLipoyl-ABH : pardp-a1bbz9Paracoccus denitrificans (strain Pd 1222) alpha/beta hydrolase fold.
Atu1826-like : pardp-a1b699Paracoccus denitrificans (strain Pd 1222) putative uncharacterized protein.
Bacterial_esterase : pardp-a1b722Paracoccus denitrificans (strain Pd 1222) Putative uncharacterized protein.
BioG_Pimeloyl-ACP-methyl-esterase : pardp-a1b660Paracoccus denitrificans (strain Pd 1222) Putative uncharacterized protein.
Carboxymethylbutenolide_lactonase : pardp-a1b7r7Paracoccus denitrificans; Paracoccus versutus (Thiobacillus versutus) 3-oxoadipate enol-lactonase, pardp-a1b193Paracoccus denitrificans (strain Pd 1222) 3-oxoadipate enol-lactonase.
DPP4N_Peptidase_S9 : pardp-a1baz8Paracoccus denitrificans (strain Pd 1222) Peptidase S9, prolyl oligopeptidase active site domain protein.
Duf_900 : pardp-a1b5s8Paracoccus denitrificans (strain Pd 1222) Putative uncharacterized protein.
FAE-Bacterial-promiscuous : parde-O54025Paracoccus denitrificans (and PD1222) orf2 protein.
Haloperoxidase : pardp-a1ayh7Paracoccus denitrificans (strain Pd 1222) alpha/beta hydrolase fold precursor.
Monoglyceridelipase_lysophospholip : pardp-a1b334Paracoccus denitrificans (strain Pd 1222) Alpha/beta hydrolase fold protein.
PhaC_cen_dom : pardp-a1b9s7Paracoccus denitrificans (strain Pd 1222) Poly-beta-hydroxybutyrate polymerase domain protein, pardp-a1bcb9Paracoccus denitrificans (strain Pd 1222) Poly-beta-hydroxybutyrate polymerase domain protein.
PHA_synth_I : parde-PHACParacoccus denitrificans (and PD1222) poly (3-hydroxyalkanoate) synthase.
PHB_depolymerase_PhaZ : parde-Q9WX79Paracoccus denitrificans, regulator for granule-associated protein and trna genes.
Proline_iminopeptidase : pardp-a1b583Paracoccus denitrificans (strain Pd 1222) Proline iminopeptidase.
UCP037442 : pardp-a1b213Paracoccus denitrificans (strain Pd 1222) Alpha/beta hydrolase

Molecular evidence		Database
No mutation No structure No kinetic No Substrate No inhibitor		2 Genbank : CP000489, AAIT01000027 1 UniProt : A1B0M3 1 UniProt : A1B0M3 1 Interpro : A1B0M3 1 Pfam : A1B0M3 1 PIRSF : A1B0M3 1 SUPERFAM : A1B0M3

Sequence

Peptide

Graphical view for this peptide sequence: pardp-a1b0m3
Colored MSA for AlphaBeta_hydrolase (raw)
MTQFLEGPQGRRIAYNRIEGQGPGVVFLGGFRSDMQGTKALWLEDWARAR GRAFLRFDYSGHGESSGMFEEGAIGDWFADAMAAIRGLTEGRQVLVGSSM GGWIGLLLARTMPERLAGLVTVAAAPDFTERGYWAGFSAAERAALLERGR VEQPSDYGDAPYVITRRLIEDGRDHLVLDQPLPLPFPVRFLQGTEDADVP MSWALDLLAHGKGEDMRLVLVKGADHRFSTPDCLALIGDALDEVLARAG
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
MTQFLEGPQGRRIAYNRIEGQGPGVVFLGGFRSDMQGTKALWLEDWARAR
GRAFLRFDYSGHGESSGMFEEGAIGDWFADAMAAIRGLTEGRQVLVGSSM
GGWIGLLLARTMPERLAGLVTVAAAPDFTERGYWAGFSAAERAALLERGR
VEQPSDYGDAPYVITRRLIEDGRDHLVLDQPLPLPFPVRFLQGTEDADVP
MSWALDLLAHGKGEDMRLVLVKGADHRFSTPDCLALIGDALDEVLARAG

No Reference

Send your questions or comments to :Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.

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