ID E6SBR6_INTC7 Unreviewed; 711 AA.
AC E6SBR6;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:ADU48425.1};
DE EC=1.1.1.35 {ECO:0000313|EMBL:ADU48425.1};
GN OrderedLocusNames=Intca_1914 {ECO:0000313|EMBL:ADU48425.1};
OS Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 / NBRC
OS 12989 / 7 KIP).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Intrasporangium.
OX NCBI_TaxID=710696 {ECO:0000313|EMBL:ADU48425.1, ECO:0000313|Proteomes:UP000008914};
RN [1] {ECO:0000313|EMBL:ADU48425.1, ECO:0000313|Proteomes:UP000008914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP
RC {ECO:0000313|Proteomes:UP000008914};
RX PubMed=21304734; DOI=10.4056/sigs.1263355;
RA Del Rio T.G., Chertkov O., Yasawong M., Lucas S., Deshpande S., Cheng J.F.,
RA Detter C., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Pukall R., Sikorski J.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Intrasporangium calvum type strain (7 KIP).";
RL Stand. Genomic Sci. 3:294-303(2010).
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; CP002343; ADU48425.1; -; Genomic_DNA.
DR RefSeq; WP_013492740.1; NC_014830.1.
DR AlphaFoldDB; E6SBR6; -.
DR STRING; 710696.Intca_1914; -.
DR KEGG; ica:Intca_1914; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_16_2_11; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000008914; 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};
KW Oxidoreductase {ECO:0000313|EMBL:ADU48425.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008914}.
FT DOMAIN 342..521
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 525..604
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 711 AA; 75215 MW; 53ADCB70A37A3FF7 CRC64;
MTATTTPAAA TPSLQFGEEV VTHAHVRDVT LPGGAGALAL ITIDNGLDHT RPTTFGPQSI
AELHAAVDAL RTRAEDGQIA AVAVTGKPFI FAVGADLTGI PLLTERDQAL AVARAGHAAF
AALADLPVPT FAFVNGAAMG GGVELALSAT YRTISSGVPA VALPEVFLGI VPGWGGCWLL
PNLVGVEKAL KVIVDNPLSQ NRMLRGPEAF SLGIADAIFE PADFLERSIA WAGGVLTGAV
TVDRPPVDRD EASWTAAVST ARRLADVKTG RHAKSPYAAL DLVAAARATT RDEGFAAEDE
ALADLIMSDE LRAGLYAFEL VQKRAKRPAG APDKALARTV TKVGIVGAGL MASQLALLFV
QRLQVPVVLT DIDDDRVAKG VGYVHAELDR LAAKGRISRD RLTRYRSLVS GSTSKAGFAD
ADFVIEAVFE EMSVKKQVFA ELEQVTGAEC VFATNTSSLS ITEMAADLQH PERVVGFHFF
NPVAVMPLLE IIPGAQTDDA TLATAFAVGK DLKKTCIRAA DRPSFIVNRL LGRFMGEAAR
IVDEGTPIEV VDRAFAGLAP MPPFVLIGLV GPAIALHNGE TLVRAFPDRF YASPTLQRLV
AAKLPGFYDL SSGRPVLTPE AAELIERPAD PVVLDVDQVR ERVLTVLADE ARRMLDEEVA
QSPMDIDLAM ITGAGFQFWN GGITPLLDRT GVAERVTGHR FLPAGVSTLP S
//
