ID A0A0A8EGM1_9ACTN Unreviewed; 709 AA.
AC A0A0A8EGM1;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Fatty acid oxidation complex alpha-subunit {ECO:0000313|EMBL:AJC55375.1};
GN ORFNames=GZL_02788 {ECO:0000313|EMBL:AJC55375.1};
OS Streptomyces sp. 769.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1262452 {ECO:0000313|EMBL:AJC55375.1, ECO:0000313|Proteomes:UP000031113};
RN [1] {ECO:0000313|EMBL:AJC55375.1, ECO:0000313|Proteomes:UP000031113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=769 {ECO:0000313|EMBL:AJC55375.1,
RC ECO:0000313|Proteomes:UP000031113};
RA Du Q., Wang Q., Li Q., Wang L., Zhang Z., Ren J., Wang J., Wang M.;
RT "Complete Genome Sequence of Streptomyces gongzhulingensis.";
RL Submitted (DEC-2012) 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; CP003987; AJC55375.1; -; Genomic_DNA.
DR RefSeq; WP_039631893.1; NZ_CP003987.1.
DR AlphaFoldDB; A0A0A8EGM1; -.
DR KEGG; stre:GZL_02788; -.
DR HOGENOM; CLU_009834_16_1_11; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000031113; 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};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027}.
FT DOMAIN 340..520
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 524..606
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 709 AA; 75396 MW; 4DF35D201E16C9DB CRC64;
MSTTAELLKG AAELFPDEVV TQAHVRHLDL PKGAGRFALI TLDNGLDHTK PTTFGPQSLA
NLNVAIDQVE KEAADGEIVG AGITGKPFIF AVGADLKGVE LLARHEDALA IGKGGHDVFK
RLSALAVPTF AYYNGAAMGG GVEVGLHCTY RTVSKALPAF SLPEVFLGLV PGWGGCALLP
NLIGADRAVS VIIENSLNQN KQLKGEQVFD LGIADALFEG ADFLERSLDW TASVLKGETE
VARPEIDRGE AWDAAVQRGK AIADSKVHGA APAAYRALDI IAAAKNGDLR QGFDAEDQAL
ADLIMGGELR SGIYAFNLVQ KRAKRPAGAP DKSLARPVTK VGVVGAGLMA SQLALLFARR
LEVPVVLTDI DQARIDKGVQ YVHGEIDKLL LKGRVNQDKA NRLKGLVSGH LDKAAAFGDA
DFVIEAVFEE MGVKQQVFAE VEAVVPEHAI LATNTSSLSV TEMASKLKHP ERVVGFHFFN
PVAILPLLEI VRAEQTDDAS LATAFAVAKS LKKTAVLVKD APAFVVNRIL TRFMGEIQNV
IDEGTPVEVA EKAVEPLGLP MSPLVLLELV GPAIGLHVSE TLHGAFPERF TVSPNLKAVV
EAGKRGFYVY DSGKPELDPE VAALLKQGDA VLTEEQVRDR VLDAVAQEIR LMLDEGVVAE
AQDIDLCLIT GAGWPFHLGG ITPYLDREGV SERVTGKKFL APGVASVPA
//
