ID M9RNG2_9RHOB Unreviewed; 733 AA.
AC M9RNG2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000313|EMBL:AGI73288.1};
DE EC=4.2.1.17 {ECO:0000313|EMBL:AGI73288.1};
DE EC=5.1.2.3 {ECO:0000313|EMBL:AGI73288.1};
GN Name=fadJ {ECO:0000313|EMBL:AGI73288.1};
GN ORFNames=OA238_c33070 {ECO:0000313|EMBL:AGI73288.1};
OS Octadecabacter arcticus 238.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Octadecabacter.
OX NCBI_TaxID=391616 {ECO:0000313|EMBL:AGI73288.1, ECO:0000313|Proteomes:UP000004688};
RN [1] {ECO:0000313|EMBL:AGI73288.1, ECO:0000313|Proteomes:UP000004688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=238 {ECO:0000313|EMBL:AGI73288.1,
RC ECO:0000313|Proteomes:UP000004688};
RX PubMed=23671678;
RA Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K.,
RA Brinkhoff T., Simon M., Daniel R.;
RT "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High Genome
RT Plasticity and a New Type of Xanthorhodopsin.";
RL PLoS ONE 8:E63422-E63422(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; CP003742; AGI73288.1; -; Genomic_DNA.
DR RefSeq; WP_015496304.1; NC_020908.1.
DR AlphaFoldDB; M9RNG2; -.
DR STRING; 391616.OA238_c33070; -.
DR KEGG; oar:OA238_c33070; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_15_2_5; -.
DR OrthoDB; 9771883at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000004688; Chromosome.
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:AGI73288.1};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AGI73288.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000004688}.
FT DOMAIN 328..506
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 510..604
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 733 AA; 78701 MW; D9F4ADE51FA9B3BE CRC64;
MTDFTMKTDA DGVAIITWDV IGKSMNVLSL QGWDDLDACV DKALADDTVK GVIITSGKKD
SFAGGMDLNI IAKMKASAGD NPAKGLMDGL MKSHSILRKI ERAGMDPKTN KGGKPIAAAL
PGTALGIGLE IPLACHRIFV ADNPKAKIGL PEIMVGIFPG MGGTTRLVRK MGAMMASPLL
LEGKMNDPKK AMQAGVVDEV VASDELLAVA KAWVLSEPKI VKPWDEKGYK MPGGEPYHPA
GFMTFVGASA MVNGKTQGVY PAAKALLSAV YEGAMVPFDT ALRIEARWFT NVLMNPSSEA
MIRSLFINKE ALDKGANRPA VADQTVKKVG VLGAGMMGAG ISLVSALAGI EVVLIDREQA
AADKGKSYTA DYMDKGIARK KATAEKKDKV LSMITATTDL NALKGCDLIV EAVFEDVGVK
AEITKKVEAI VGDDCIFATN TSTLPITELA KASVRPDQFI GIHFFSPVDK MALVEIIRGK
ETGDIAVAKS LDFVRQIRKT PIVVNDERFF YANRCILPYV NEGVRMLQEG VAPALIENAA
KLVGMPLGPL QLTDETSIDL GVKIAKATKA AMGDAYDDTA DELIFWMADE GRLGRKTKAG
FYDYDEKGKR HYLWSGLTER YAPADEQPDL VDVQHRLLFS QVLEAVRALD EGVLMDIREG
DVGAILGWGF APWSGGPFSW LDILGAPYAA ERCDELTAIH GERFACPALL RDMADKGQSF
YGRFGSGVDS KAA
//
