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Database: UniProt
Entry: S6GK87_9GAMM
LinkDB: S6GK87_9GAMM
Original site: S6GK87_9GAMM 
ID   S6GK87_9GAMM            Unreviewed;       775 AA.
AC   S6GK87;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:EPJ49296.1};
GN   ORFNames=OFPII_01780 {ECO:0000313|EMBL:EPJ49296.1};
OS   Osedax symbiont Rs1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae.
OX   NCBI_TaxID=1330036 {ECO:0000313|EMBL:EPJ49296.1, ECO:0000313|Proteomes:UP000014822};
RN   [1] {ECO:0000313|EMBL:EPJ49296.1, ECO:0000313|Proteomes:UP000014822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rs1 {ECO:0000313|Proteomes:UP000014822};
RA   Yi H., Goffredi S.;
RT   "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT   Osedax worms: functional variation and environmental selection.";
RL   Submitted (MAY-2013) 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:EPJ49296.1}.
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DR   EMBL; ASZJ01000012; EPJ49296.1; -; Genomic_DNA.
DR   AlphaFoldDB; S6GK87; -.
DR   PATRIC; fig|1330036.3.peg.164; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000014822; 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; 2.
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   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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014822}.
FT   DOMAIN          6..189
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          192..293
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   DOMAIN          347..397
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   775 AA;  84839 MW;  CC3287A6933B1026 CRC64;
     MSAINKVCVI GAGVMGASIA AHIANAGYPV LLLDIVPVAA KNRNIIAQTA IQKLLKSNPA
     ALTHPRNAKL ITPLNIEDHL DQLSDCDWII EAIVERLDIK QELYKKLDQH RKSGSIVSSN
     TSTIPLTSLA SGMSASFSED FCITHFFNPP RYMRLLEVVK GTDTRQSAID TVSEFADYKL
     GKSIVNCKDR PGFIANRLGI FWIYCALVEA FDCGMSIEEA DAVLSRPCGV PKTGVFGLID
     LVGLDLMPNI LQSMVSLLPE NDPFVQIERS LPLLEKMISD GYTGRKGKGG FYRINRDGGG
     KVKEAIDLVS GEYRPVLKVE SQCAKIKVKD IRQLFETNDK SAKYAWRVMS QTLAYAASLV
     ADAAEDITAI DEAMRLGYNW KFGPFKLLDI LGPQWFIEKL EQQNQVVPPI LQKLSGKSFY
     REQEQKLQYF TSTGNYRDLQ RPSGILMLAD IKRRSQPILK NASAALWDIG DGVACFEFTS
     KMNSLDSDTM QLLQKSILTV SKSYAALVIY TDANNFSAGA NLGLAMFAAN IAAWPEIAKI
     VAAGQQAYKA LKYSPFPVVS APCGMALGGG CEILLHCDAV QAHIETYTGL VEVGVGLVPA
     WGGCKEMLHR WSTNPKHPRG PMPGPAKAFE LISTATVSKS AEEARSNMVL RDTDGITMNR
     YRLLSDAKQK ALSLVADYQA PQAPTFHLPG PSAKAAFTMA VDGFVRSGKA TKHDRVVSMA
     VADILSGGAK ADPTVEQSED EILALERKTF MKIIRHPDSL ERVEHILLTS KPLRN
//
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