ID A0A0M7B7M6_9RHOB Unreviewed; 729 AA.
AC A0A0M7B7M6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000313|EMBL:CUH26794.1};
GN Name=fadJ_1 {ECO:0000313|EMBL:CUH26794.1};
GN ORFNames=JSE7799_00753 {ECO:0000313|EMBL:CUH26794.1};
OS Jannaschia seosinensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=313367 {ECO:0000313|EMBL:CUH26794.1, ECO:0000313|Proteomes:UP000049455};
RN [1] {ECO:0000313|EMBL:CUH26794.1, ECO:0000313|Proteomes:UP000049455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7799 {ECO:0000313|EMBL:CUH26794.1,
RC ECO:0000313|Proteomes:UP000049455};
RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL Submitted (SEP-2015) 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}.
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DR EMBL; CYPR01000043; CUH26794.1; -; Genomic_DNA.
DR RefSeq; WP_055662416.1; NZ_CYPR01000043.1.
DR AlphaFoldDB; A0A0M7B7M6; -.
DR STRING; 313367.JSE7799_00753; -.
DR OrthoDB; 9771883at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000049455; 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; 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 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:UP000049455}.
FT DOMAIN 327..505
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 509..604
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 633..718
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 729 AA; 77890 MW; B77C17650AD5F65C CRC64;
MTDFTLSKDA DGVATITWDV AGKSMNVLSL EGWEHLETCI DDALADDAVK GIVITSGKDS
FAGGMDLNVI ARMKAEAGDD PARGLFDGLM RSHAILRKLE RAGMDPKTLK GGKPVACVLP
GTALGIGFEI PLACHRIFAA DNPKAKIGLP EIMVGIFPGM GGTTRLARKL GAMAASPFLL
EGKLSDPKKA KAAGLIDEVT DDPMAAAREW VLQAKDSDIV KPWDAKGYKM PGGAPYHPAG
FMTFVGASAM VNGKTQGAFP AAKALLSAVY EGALVPFDTA LKIEARWFTH VLMNPSSEAM
IRSLFINKEA LEKGANRPDA PDQKVRKVGV LGAGMMGAGI AYVSANAGIE VVLVDREQAA
AEKGKDYSAE LLDKGIARKK VTGEKKDEVL SRIHATTDLD ALKGCDLIVE AVFEDVGVKA
EMTQKVEAVV GEEAIFATNT STLPITELAK ASARPEQFIG IHFFSPVDKM LLVEIIKGRD
TGDRAVAKAL DYVRQIRKTP IVVNDARFFY ANRCIIPYIN EGIRMVAEGV SPALIENAAK
QLGFPLGPLQ LVDETSIDLG VKIAKATKAA MGDAYPDAAV DEVLFAFADA GRLGRKASAG
FYDYDEKGKR QGLWAELGAR YPLAEEQPDL HHVQNRLMFA QVLEAVRALE EGVLEDIREG
DVGAILGWGF APWSGGPFSW LDIVGAAWAA ETTAALAETH GPRFATPKLL SDMATEGRTF
YGARSRNAA
//
