ID D9SZP4_MICAI Unreviewed; 687 AA.
AC D9SZP4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase NAD-binding {ECO:0000313|EMBL:ADL45176.1};
GN OrderedLocusNames=Micau_1621 {ECO:0000313|EMBL:ADL45176.1};
OS Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 / CBS
OS 129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=644283 {ECO:0000313|EMBL:ADL45176.1, ECO:0000313|Proteomes:UP000001908};
RN [1] {ECO:0000313|EMBL:ADL45176.1, ECO:0000313|Proteomes:UP000001908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442
RC {ECO:0000313|Proteomes:UP000001908};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Hirsch A.M., Woyke T.;
RT "Complete sequence of Micromonospora aurantiaca ATCC 27029.";
RL Submitted (AUG-2010) 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; CP002162; ADL45176.1; -; Genomic_DNA.
DR RefSeq; WP_013284814.1; NC_014391.1.
DR AlphaFoldDB; D9SZP4; -.
DR STRING; 644283.Micau_1621; -.
DR KEGG; mau:Micau_1621; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_16_2_11; -.
DR OrthoDB; 3216872at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000001908; 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; -; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001908}.
FT DOMAIN 325..504
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 508..587
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 687 AA; 73266 MW; 7FB0D53FB4F3EA1B CRC64;
MSLAAPNEVV TKALLRQVAV PGLDRPAALI TLDNGFDHTK PNTFGPAGLT SLDEAITAAL
SAEPAFIAVT GKPYIFCVGA DITSLPALEN REQALEIGRL GHRVFARLKD SGVPTFAFVN
GAAMGGGLEL ALHCHYRTLS AGAAALALPE VSLGLIPGWG GTQLLPNLIG IPAATQVIIQ
NPLMQNKMLK PKQAAEMGIA DVLLEPADFL ERSLEWAAGV VRGEVTVTRP EVDKDMWAGV
LYFARQTLDQ RLHGAVPSAY KALDLLETAK DADFATGTAA EDEALADLVF SEELRSGLYA
FDLVQRRAKR PAGAPDKGLA RPVTKVGIVG AGLMASQLAL LFARRLQVPV VMTDLDQSRV
DKGVGYVHTQ IEKAVSKGRM DKGTAAKLYG LVSGSVDKSV FADADFVIEA VFEDLGVKKQ
VWAELEKIVK PEAVLATNTS SLSITEMAAE LEHPERVVGF HFFNPVAVLP LLEIVRGERT
DDATLATAFA VGKQLRKSSV LVKDAPAFVV NRLLTRFLGT VFAAVDQGTP LDVANSALDP
LGLPMRPLAL LQLVGPAVAY HVGGTLHEAF PDRFGVSENL KRIADSGQPI VVDDQINDEV
AKLLVVGDEP LTAEQVRQNA LDALAQEIRL MLDEGVVAEA QDIDLCMILG AGWPFHLGGV
TPYLDRTGTS ERVTGKRFLP HGVASLR
//
