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Database: UniProt
Entry: B8KTR7_9GAMM
LinkDB: B8KTR7_9GAMM
Original site: B8KTR7_9GAMM 
ID   B8KTR7_9GAMM            Unreviewed;       715 AA.
AC   B8KTR7;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   SubName: Full=Fatty acid oxidation complex, alpha subunit {ECO:0000313|EMBL:EED34528.1};
DE            EC=1.1.1.35 {ECO:0000313|EMBL:EED34528.1};
DE            EC=4.2.1.17 {ECO:0000313|EMBL:EED34528.1};
DE            EC=5.1.2.3 {ECO:0000313|EMBL:EED34528.1};
GN   Name=fadJ {ECO:0000313|EMBL:EED34528.1};
GN   ORFNames=NOR51B_465 {ECO:0000313|EMBL:EED34528.1};
OS   Luminiphilus syltensis NOR5-1B.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC   Luminiphilus.
OX   NCBI_TaxID=565045 {ECO:0000313|EMBL:EED34528.1, ECO:0000313|Proteomes:UP000004699};
RN   [1] {ECO:0000313|Proteomes:UP000004699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NOR51-B {ECO:0000313|Proteomes:UP000004699};
RX   PubMed=23705883;
RA   Spring S., Riedel T., Sproer C., Yan S., Harder J., Fuchs B.M.;
RT   "Taxonomy and evolution of bacteriochlorophyll a-containing members of the
RT   OM60/NOR5 clade of marine gammaproteobacteria: description of Luminiphilus
RT   syltensis gen. nov., sp. nov., reclassification of Haliea rubra as
RT   Pseudohaliea rubra gen. nov., comb. nov., and emendation of Chromatocurvus
RT   halotolerans.";
RL   BMC Microbiol. 13:118-118(2013).
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; DS999411; EED34528.1; -; Genomic_DNA.
DR   RefSeq; WP_009019276.1; NZ_DS999411.1.
DR   AlphaFoldDB; B8KTR7; -.
DR   STRING; 565045.NOR51B_465; -.
DR   eggNOG; COG1024; Bacteria.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_009834_15_3_6; -.
DR   OrthoDB; 5389341at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000004699; Unassembled WGS sequence.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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   Isomerase {ECO:0000313|EMBL:EED34528.1};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:EED34528.1};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EED34528.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004699}.
FT   DOMAIN          319..497
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          500..599
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   715 AA;  77234 MW;  75C7C4E3E8EAB4D9 CRC64;
     MSGFNYEKDG DGIVTITMDM DGPVNSMSAE YGPMMKATVD RLEAESDLTG VVIASAKKTF
     FAGGDLKMLA QVTSETAGEF FEGCEAVKAD LRRLERLPVP VAAAINGAAL GGGLEICLAC
     NYRVAWDDKS VKLGLPEVTL GLLPGGGGIV RMIHLLGLMA SNEFLLEGKQ VDPARAKEAG
     IIHEVVASRD ELVGLAKAWI LANKDNEDAA VQPWDRKGHK IPGGNANTPS LAQMIPAAAP
     MLIKKTRGLL PAPEKILDVA VSALRVDFDT ALRIESRGLT YLVQTAVAKN MINTFFFQLN
     KVNGGASRPS DVEPQATKKV GVLGAGMMGQ GIAYVSAMAG IEVVLKDIDK DAAIKGKGYS
     EKLLQKRVDK GRMTAEKMQE VLALITPSAD NADLEGCDLI IEAVFENMTL KHKITKETEP
     CLAEGGVWGS NTSTLPITEL AEASINPENF IGIHFFSPVD KMPLVEIICG EQTGDVALAK
     AFDFARQIRK TPIVVNDSLG FFTSRTFATY LEEGARLVME GLHPIKIDNL GKAIGMPVGP
     LTIQDEVSQE LSRKAQATWV ELGYADRFGD QSQYRDFIDW MVLENDRGGR HHGGGYYDYH
     ADGSKTLWPV VVDKYYKPEV SLADEDVKDR LLFRQVIEAL KCLESGVLRT VADGNVGSIM
     GIGAPVWTGG FIQFVNTYGL DKFIARCEEL SAAYGDRFDP PAIVAEKLAA GENFS
//
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