ID A0A2D3US15_9PEZI Unreviewed; 311 AA.
AC A0A2D3US15;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 11.
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};
GN ORFNames=RCC_00324 {ECO:0000313|EMBL:CZT14347.1};
OS Ramularia collo-cygni.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Ramularia.
OX NCBI_TaxID=112498 {ECO:0000313|EMBL:CZT14347.1, ECO:0000313|Proteomes:UP000225277};
RN [1] {ECO:0000313|EMBL:CZT14347.1, ECO:0000313|Proteomes:UP000225277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=URUG2 {ECO:0000313|EMBL:CZT14347.1,
RC ECO:0000313|Proteomes:UP000225277};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009463}.
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DR EMBL; FJUY01000001; CZT14347.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2D3US15; -.
DR STRING; 112498.A0A2D3US15; -.
DR OrthoDB; 5402028at2759; -.
DR Proteomes; UP000225277; Unassembled WGS sequence.
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; IPR006180; 3-OHacyl-CoA_DH_CS.
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.
DR PROSITE; PS00067; 3HCDH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000225277}.
FT DOMAIN 7..180
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 183..251
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT SITE 136
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ SEQUENCE 311 AA; 34244 MW; 5C9E2815B5C7849D CRC64;
MATRSNTVAI VGAGTIGLSF AALHLTKDPS CKVAIFDNRS DLQAYVSEHL PRYLVDADRD
TCFARLTLAE SLEEAVRDAD IVQEQGPENA SFKIQIWPEI EQYAPQKALF WSSTSGIPAS
EQVRDMQDKS RLLVCHPYNP PHIMPLLEVV RSPDTSDDVV ERTLSYWRNL GRAPVVIRKE
CVGFVANRLA FALFREACSL VAQGVVGVED LDEIVRTSMG PRWTVAGPFK SYHAGGGEGG
LTSFMAKIGD TVQGCWNASD EDMKRGNIVV GGPWQDDVCK QTQEAYGMVN TSERDLKTRN
ILSAVKDSCR A
//