ID X5EDF8_9CORY Unreviewed; 761 AA.
AC X5EDF8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase / short chain enoyl-CoA hydratase {ECO:0000313|EMBL:AHW65425.1};
DE EC=4.2.1.17 {ECO:0000313|EMBL:AHW65425.1};
GN Name=fadB4 {ECO:0000313|EMBL:AHW65425.1};
GN ORFNames=CGLY_14945 {ECO:0000313|EMBL:AHW65425.1};
OS Corynebacterium glyciniphilum AJ 3170.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1404245 {ECO:0000313|EMBL:AHW65425.1, ECO:0000313|Proteomes:UP000023703};
RN [1] {ECO:0000313|EMBL:AHW65425.1, ECO:0000313|Proteomes:UP000023703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AJ 3170 {ECO:0000313|EMBL:AHW65425.1};
RX PubMed=25323597; DOI=10.1099/ijs.0.065102-0;
RA Al-Dilaimi A., Bednarz H., Lomker A., Niehaus K., Kalinowski J.,
RA Ruckert C.;
RT "Revisiting Corynebacterium glyciniphilum (ex Kubota et al., 1972) sp.
RT nov., nom. rev., isolated from putrefied banana.";
RL Int. J. Syst. Evol. Microbiol. 65:177-182(2015).
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; CP006842; AHW65425.1; -; Genomic_DNA.
DR RefSeq; WP_038550448.1; NZ_CP006842.1.
DR AlphaFoldDB; X5EDF8; -.
DR STRING; 1404245.CGLY_14945; -.
DR KEGG; cgy:CGLY_14945; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_16_3_11; -.
DR OrthoDB; 9771883at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000023703; Chromosome.
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; 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, ECO:0000313|EMBL:AHW65425.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000023703}.
FT DOMAIN 328..506
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 509..609
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 761 AA; 79995 MW; 28143AD784B4C074 CRC64;
MSDNIIAWET DGNGVVTLTI DDPSSSVNTM NDAFRDSVKE TAEKLQSGVE AGDVKGVVIT
SAKKTFFAGG DIKSMITATP ADAPALQKQI DQMKADMRTI ETLGVPVVAA LNGTALGGGL
EIALATHHRI AADTRGAKFG LPEVTLGLLP GGGGVARVTR MLGIQDALMK VLTTGRQFSA
EAAKDTGLID EIVPADQLID AAKAWIASEP DASQPWDRKG YRMPGGTPTT PALAAMLPSF
PANVTKQIKG APMPAPQAIL SAAVEGAQLK RFEDATAVET RWFVSLVTGP TSKNMMQAFF
FDLNHCNGGG SRPVQEDGTP YPKTEFRKVG VIGAGMMGAG IAYVAAKAGI EVVLKDISEE
NAQKGKAYSE GLEAKALKRG KTTEEKSAAL LGRITPTADY ADLSDVDLVI EAVFENTELK
HKVFAEIEAA VPSTAVLGSN TSTLPITGLA EGVDRQNDFI GLHFFSPVDK MPLIEIISGE
KTDPAVLAKA LDFARQIRKT PIVVNDSRGF FTSRVIGTVL NEAMRMLVEG VDPAVIEAAG
RQAGYPAPQL QLQDELNLKL ARKIGAETAA AAKAAGVSVD DGGVNALVDA MLDDFDRPGK
LEGKGFYEYD ENGRRAGLWS GLRGEVRDKL GITPVTVPDG EAATAGADLN STTGDGAPTL
NDLIERMLFI EALETQRCID ENVLTSDADA NIGSILGIGY PAWTGGSRQF ISNYARPAAA
PLPADAGDDY PTSGVAGFVA RAEELATAYG ERFAPLESLK G
//
