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Database: UniProt
Entry: W9VVI6_9EURO
LinkDB: W9VVI6_9EURO
Original site: W9VVI6_9EURO 
ID   W9VVI6_9EURO            Unreviewed;       317 AA.
AC   W9VVI6;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=3-hydroxybutyryl-CoA dehydrogenase {ECO:0000313|EMBL:EXJ59797.1};
GN   ORFNames=A1O7_03944 {ECO:0000313|EMBL:EXJ59797.1};
OS   Cladophialophora yegresii CBS 114405.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=1182544 {ECO:0000313|EMBL:EXJ59797.1, ECO:0000313|Proteomes:UP000019473};
RN   [1] {ECO:0000313|EMBL:EXJ59797.1, ECO:0000313|Proteomes:UP000019473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114405 {ECO:0000313|EMBL:EXJ59797.1,
RC   ECO:0000313|Proteomes:UP000019473};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., 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 Cladophialophora yegresii CBS 114405.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC       {ECO:0000256|ARBA:ARBA00005086}.
CC   -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009463}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXJ59797.1}.
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DR   EMBL; AMGW01000003; EXJ59797.1; -; Genomic_DNA.
DR   RefSeq; XP_007756150.1; XM_007757960.1.
DR   AlphaFoldDB; W9VVI6; -.
DR   STRING; 1182544.W9VVI6; -.
DR   GeneID; 19178535; -.
DR   VEuPathDB; FungiDB:A1O7_03944; -.
DR   eggNOG; KOG2304; Eukaryota.
DR   HOGENOM; CLU_009834_2_0_1; -.
DR   OrthoDB; 314530at2759; -.
DR   Proteomes; UP000019473; 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:SF5; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 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   NAD {ECO:0000256|PIRSR:PIRSR000105-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019473}.
FT   DOMAIN          32..215
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          221..317
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   BINDING         37..42
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         61
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         120
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         125
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         147
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         178
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   BINDING         309
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT   SITE            175
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ   SEQUENCE   317 AA;  33916 MW;  569E6B7E63708CBD CRC64;
     MASSKSQVAS QRLASLNRQF SSSPSKAFEV KKLGVIGAGQ MGLGIALVAA QKAQVSVTLV
     DNSQQSLEKG LAFADKLLAK DVQKQRITEE IAKATRERLK STTNISDLSD VDMVIEAVPE
     IPSLKEKIFA DLAQICPKHA ILATNTSSIS ITRIARATAK DPTDTQASSR VVSTHFMNPV
     PVQKGVEIIA GLQTSPETVT AAIAFCEKMG KVASVSADSP GFLANRILMP YINEAIICLE
     TGVGNKEDID NIMKNGTNVP MGPLTLADFI GLDTCLAIME TLHAGLGDSK YRPSVLLRQY
     VDAGWLGKKS GRGFYEY
//
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