ID A0A182WVZ1_ANOQN Unreviewed; 285 AA.
AC A0A182WVZ1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=omega-amidase {ECO:0000256|ARBA:ARBA00039118};
DE EC=3.5.1.3 {ECO:0000256|ARBA:ARBA00039118};
DE AltName: Full=Nitrilase homolog 2 {ECO:0000256|ARBA:ARBA00041576};
OS Anopheles quadriannulatus (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=34691 {ECO:0000313|EnsemblMetazoa:AQUA001697-PA, ECO:0000313|Proteomes:UP000076407};
RN [1] {ECO:0000313|Proteomes:UP000076407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SANGQUA {ECO:0000313|Proteomes:UP000076407};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles quadriannulatus QUAD4_A.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AQUA001697-PA}
RP IDENTIFICATION.
RC STRAIN=SANGQUA {ECO:0000313|EnsemblMetazoa:AQUA001697-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutaramate + H2O = 2-oxoglutarate + NH4(+);
CC Xref=Rhea:RHEA:32963, ChEBI:CHEBI:15377, ChEBI:CHEBI:16769,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938; EC=3.5.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00036637};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32964;
CC Evidence={ECO:0000256|ARBA:ARBA00036637};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxosuccinamate + H2O = NH4(+) + oxaloacetate;
CC Xref=Rhea:RHEA:59412, ChEBI:CHEBI:15377, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:57735; EC=3.5.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00036705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59413;
CC Evidence={ECO:0000256|ARBA:ARBA00036705};
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DR AlphaFoldDB; A0A182WVZ1; -.
DR STRING; 34691.A0A182WVZ1; -.
DR EnsemblMetazoa; AQUA001697-RA; AQUA001697-PA; AQUA001697.
DR VEuPathDB; VectorBase:AQUA001697; -.
DR Proteomes; UP000076407; Unassembled WGS sequence.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR CDD; cd07572; nit; 1.
DR Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR045254; Nit1/2_C-N_Hydrolase.
DR PANTHER; PTHR23088; NITRILASE-RELATED; 1.
DR PANTHER; PTHR23088:SF30; OMEGA-AMIDASE NIT2; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 9..257
FT /note="CN hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS50263"
SQ SEQUENCE 285 AA; 31090 MW; 8AC6DC04D9BD39AF CRC64;
MNRMARAGFR IALLQLKVGA DKAQNIENAL AKIRSAVADK GARVVALPEC FNSPYGTQHF
PAYAEEIPSG ETSRSLAAIA KELGIYLIGG TIPEKCRTDS KLYNTCTVWS PEGSLLATYR
KIHLFDINIP GGITFRESDV LTGGSTLATV AIDGAKVGLG ICYDMRFDEL ARLYRNQGCD
MLIYPGAFNM KTGPLHWELL ARGRANDTQS YVATISPARD PSAGYVAWGH SMVVDPWAKV
VAEANEEEAT VVADVNLQTV DEVRAQIPIF SQRRTDLYAT NALEK
//
