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Database: UniProt
Entry: A0A1V1ZGF4_9FLAO
LinkDB: A0A1V1ZGF4_9FLAO
Original site: A0A1V1ZGF4_9FLAO 
ID   A0A1V1ZGF4_9FLAO        Unreviewed;       802 AA.
AC   A0A1V1ZGF4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:OMP31221.1};
GN   ORFNames=BKM32_09190 {ECO:0000313|EMBL:OMP31221.1};
OS   Mangrovimonas sp. DI 80.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Mangrovimonas.
OX   NCBI_TaxID=1779330 {ECO:0000313|EMBL:OMP31221.1, ECO:0000313|Proteomes:UP000188854};
RN   [1] {ECO:0000313|EMBL:OMP31221.1, ECO:0000313|Proteomes:UP000188854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DI 80 {ECO:0000313|EMBL:OMP31221.1,
RC   ECO:0000313|Proteomes:UP000188854};
RA   Krishnamurthi S., Pal Y., Verma A., Sundharam S.;
RT   "Taxonomic characterization of strain DI 80 closely related to
RT   Mangrovimonas sp.";
RL   Submitted (DEC-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   -!- 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:OMP31221.1}.
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DR   EMBL; MSDT01000004; OMP31221.1; -; Genomic_DNA.
DR   RefSeq; WP_076663540.1; NZ_MSDT01000004.1.
DR   AlphaFoldDB; A0A1V1ZGF4; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000188854; Unassembled WGS sequence.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR48075:SF7; 3-HYDROXYACYL-COA DEHYDROGENASE-RELATED; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188854}.
FT   DOMAIN          8..206
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          209..308
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   802 AA;  88433 MW;  3183FF590B3CF3FC CRC64;
     MSKRIIKKVA VIGSGIMGSG IACHFANIGV EVLLLDIVPR ELNDIEKTKG LTLNDAVVRN
     RLVNDALKAA LKSKPSPIYH QSFANRIQTG NLEDDIAKVA NVDWIIEVVV ERLDIKKSVF
     ENLEKHRTPG TLITSNTSGI PIHFMSEGRS EDFQKHFCGT HFFNPARYLK LFEIIPGPKT
     SPEVLEFLNG YGEQYLGKTS VVAKDTPAFI GNRIGIFGIM SLFHQVKALG LTIEEVDKLT
     GPVIGRPKSA TFRTVDVVGL DTLVHVANGL YENCPNDEAH ELFKLPGFIN TMMENKWLGS
     KTGQGFYKKV KADDGSSEIL SLDLDTLEYR SKKSAKFATL ELTKTVDKVI DRFPILVSGK
     DKAGEFYRKN FAAMFAYVSH RIPEITKELY KIDDAMKAGF GWEHGPFQIW DAIGLAKGIE
     LMQQEGLEPA PWVSDMLSSG STSFYTVKDG ATYCYDIPSK TQLKVPGQDA FIILDNIRKS
     NEVFKNSGVV IEDLGDGILN CEFQSKMNTI GGDVLAGINK AIDLAEKDFD GLVIGNQGAN
     FSVGANIGMI FMMAVEQEYD ELNMAIKYFQ DTMMRMRYSS IPTISAPHGM TLGGGCELSL
     HADKVVAAAE TYMGLVEFGV GVIPGGGGSK EMTLRASDTF RKNDVELNVL QEYFMAIGMA
     KVSTSAYEAF DFGVLQKGKD VVVVNKDRQI ATAKAYARLM ADQGYTQPIK RNDVKVLGKQ
     ALGMFLVGID SMQAGHYISE HDKKIATKLA YVMAGGDLSE ASLVSEQYLL DLEREAFLSL
     CTERKTLERI QHMLKTGKPL RN
//
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