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Database: UniProt
Entry: A0A1Q3GM82_9BACT
LinkDB: A0A1Q3GM82_9BACT
Original site: A0A1Q3GM82_9BACT 
ID   A0A1Q3GM82_9BACT        Unreviewed;       730 AA.
AC   A0A1Q3GM82;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:OJJ16960.1};
GN   ORFNames=BKI52_30040 {ECO:0000313|EMBL:OJJ16960.1};
OS   marine bacterium AO1-C.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae.
OX   NCBI_TaxID=1905359 {ECO:0000313|EMBL:OJJ16960.1, ECO:0000313|Proteomes:UP000186474};
RN   [1] {ECO:0000313|EMBL:OJJ16960.1, ECO:0000313|Proteomes:UP000186474}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AO1-C {ECO:0000313|EMBL:OJJ16960.1};
RA   Buerger P., Wood-Charlson E.M., Weynberg K.D., Willis B., Van Oppen M.J.;
RT   "CRISPR-Cas defence system in Roseofilum reptotaenium: evidence of a
RT   bacteriophage-cyanobacterium arms race in the coral black band disease.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC         NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
CC         Evidence={ECO:0000256|ARBA:ARBA00023693};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005005}.
CC   -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005}.
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:OJJ16960.1}.
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DR   EMBL; MLAY01000011; OJJ16960.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3GM82; -.
DR   STRING; 1905359.BKI52_30040; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000186474; Unassembled WGS sequence.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   CDD; cd06558; crotonase-like; 1.
DR   Gene3D; 1.10.1040.50; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR43612:SF3; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186474}.
FT   DOMAIN          326..504
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          507..604
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   730 AA;  80095 MW;  D79956227FAE8098 CRC64;
     MVLYNVEEGV AIISWNMEGY TMNVLNEDSI KAFADAVEKA VGDEAVKGII ITSEKETFGA
     GADLKMIKSM LNQQNLDVKT AFENARQLNQ LFRSYETSGK PVVAGINGTA LGGFYEVCLA
     CHYRVAVNNP KSKIGLPESQ VGLIPGAGGT QRVPRMVGIE AAAPLLLEGK TLSPERALKA
     GLVDEVVADK AQMMAAAKKF IAENKFIMQP WDEKNRKGQI VGKKNFRVPK GNIQSPKGVQ
     VLMPGTALLM DKTKGNYPAQ LAIMSCVYEG LQVPMDQALD IESRHFTRIL RTPEAKGMVR
     TLFFGKQAAD KGEARPKDVP KYDIKTVAVL GAGMMGAGIA YVSAMAGMKV VLKDISVENA
     EKGKDYSRNL LKKRVSKKRM TQEKADAVLE LIHPTADYAD LAEADYVIEA VFENRDLKYK
     VTQEVEAVIR EDVIFGSNTS TLPITGLAEA SKRPDQFIGI HFFSPVDKMM LVEVIMGEKS
     SDKALAATLD YIQKIKKTPI VVNDSRGFYT SRCFSTYTAE GMEMLQEGIN PILIENAGKA
     AGMPVGPLDV ADAVALDLAY KIMKQTSKDL GQPMEDMPGG KVVIKFNEEL DRVGKKAKKG
     FYAYPENGKK YLWEGLQEHY PLAENQPDIE TLKKRFLHRQ AMECIRCLEE GVLRNPTDGD
     IGSIFAWGFA PFTGGAFSYV DAVGIAQFVK DCDEFEAQFG ERFKVSDKLR AMAANGESFF
     KEEAVEAAAV
//
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