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Database: UniProt
Entry: F5RDE6_METUF
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ID   F5RDE6_METUF            Unreviewed;       667 AA.
AC   F5RDE6;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Alpha-subunit of fatty acid oxidation complex {ECO:0000313|EMBL:EGK70927.1};
GN   ORFNames=METUNv1_02313 {ECO:0000313|EMBL:EGK70927.1};
OS   Methyloversatilis universalis (strain ATCC BAA-1314 / JCM 13912 / FAM5).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Sterolibacteriaceae; Methyloversatilis.
OX   NCBI_TaxID=1000565 {ECO:0000313|EMBL:EGK70927.1, ECO:0000313|Proteomes:UP000005019};
RN   [1] {ECO:0000313|EMBL:EGK70927.1, ECO:0000313|Proteomes:UP000005019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1314 / JCM 13912 / FAM5
RC   {ECO:0000313|Proteomes:UP000005019};
RX   PubMed=21725020; DOI=10.1128/JB.05331-11;
RA   Kittichotirat W., Good N.M., Hall R., Bringel F., Lajus A., Medigue C.,
RA   Smalley N.E., Beck D., Bumgarner R., Vuilleumier S., Kalyuzhnaya M.G.;
RT   "Genome sequence of Methyloversatilis universalis FAM5T, a methylotrophic
RT   representative of the order Rhodocyclales.";
RL   J. Bacteriol. 193:4541-4542(2011).
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}.
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:EGK70927.1}.
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DR   EMBL; AFHG01000052; EGK70927.1; -; Genomic_DNA.
DR   RefSeq; WP_008061805.1; NZ_AFHG01000052.1.
DR   AlphaFoldDB; F5RDE6; -.
DR   STRING; 1000565.METUNv1_02313; -.
DR   eggNOG; COG1024; Bacteria.
DR   eggNOG; COG1250; Bacteria.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000005019; 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; 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; IPR013328; 6PGD_dom2.
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   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:UP000005019}.
FT   DOMAIN          316..488
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          493..582
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   667 AA;  70327 MW;  645D65D6D41DE849 CRC64;
     MTAEMSVQAN TFRHWRLERD AGDVAWLTFD RAGEHVNTLS GEAMRELGAV LDALDAAPPK
     GLVILSGKAG GFIAGADIGE FGAVKDEAGA RDIVGRGWNL FNRLAAVPYP TCALVRGFCV
     GGGTELALAC RHIVAVDEPG TRFALPEVLL GIVPGWGGML RLPQRIGAPA ALDMMLTGRA
     LDAKRAKAAG LVDEIAPARL MREHARARVL ADPPRRALPL LQRLLLGPLR GTVAKKALEG
     VAKKAARRHY PAPYAIVEIW RDFGGNALAV PAAHPASMAS LVAHPTTASL QRVYHLRERL
     RGFAKADSAL PPIRRVHVVG AGVMGGDIAA WCALRGFHVT LQDNGLERIA PAMQRAAKAF
     ARKFRRDRKA LRDALDRLVP DPTGAAAAGA DLIIEAIYED LEAKQTLLAD VERRAKPEAL
     IATNTSSLRI EDIARALQAP SRLVGIHFFN PVAKMPLVEV VRGAGSTDSA VQRAAAFVGA
     LDKLPLPVGS APGFLVNAVL GPYMLEAMKC MDEGLPPEVV DRAALDFGMA MGPVELADTV
     GLDIAMAAGS RLTGGAAAPA CLQARVEQGH LGRKTGQGFY AWKDGHPERA QPAAVPAGLT
     ERLLAPLIQV TRRCVDNAVV GDADLADAGL VFGAGFAPYT GGPLHYDAAS HPGRSASGTV
     LNAHHAH
//
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