ID A0A182K2A6_9DIPT Unreviewed; 311 AA.
AC A0A182K2A6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=L-gulonate 3-dehydrogenase {ECO:0000256|ARBA:ARBA00038962};
DE EC=1.1.1.45 {ECO:0000256|ARBA:ARBA00038962};
DE AltName: Full=L-gulonate 3-dehydrogenase {ECO:0000256|ARBA:ARBA00042709};
OS Anopheles christyi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43041 {ECO:0000313|EnsemblMetazoa:ACHR004890-PA, ECO:0000313|Proteomes:UP000075881};
RN [1] {ECO:0000313|Proteomes:UP000075881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACHKN1017 {ECO:0000313|Proteomes:UP000075881};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., 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 christyi ACHKN1017.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACHR004890-PA}
RP IDENTIFICATION.
RC STRAIN=ACHKN1017 {ECO:0000313|EnsemblMetazoa:ACHR004890-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009463}.
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DR AlphaFoldDB; A0A182K2A6; -.
DR STRING; 43041.A0A182K2A6; -.
DR EnsemblMetazoa; ACHR004890-RA; ACHR004890-PA; ACHR004890.
DR VEuPathDB; VectorBase:ACHR004890; -.
DR OrthoDB; 5402028at2759; -.
DR Proteomes; UP000075881; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR022694; 3-OHacyl-CoA_DH.
DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR InterPro; IPR006108; 3HC_DH_C.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR48075:SF1; LAMBDA-CRYSTALLIN HOMOLOG; 1.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR PIRSF; PIRSF000105; HCDH; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 5..183
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 189..278
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT SITE 142
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ SEQUENCE 311 AA; 34708 MW; FA402E1331171F1F CRC64;
MKKEKVAIIG SGLIGRSWAM LFAGVGYQVT IYDIIPDIVE KALKETKQEL DSIEKQGFLR
GNLTASEQFA CISGTDNLKD AITDAIYVQE CVPERLDIKK KLYAEVDGLV GPNTILASST
STFMPSLFSE DMKHRAQVLV AHPVNPPYYV PLVEIVPAPW TKAEYTTKAR ELMTEIGQKP
VTLSRQIEGF ALNRIQYAIL NETWRLVADG ILSVKDIDVV MSEGLGMRYA FLGPLETAHL
NAEGMLNYCD RYCNTIYAVS QTMGPTPRME GKVAEQVAKE LDEMVPIDKL PERRAWRDAC
LTKLAQLKKT I
//