ID I3TXA5_TISMK Unreviewed; 777 AA.
AC I3TXA5;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:AFK57393.1};
GN Name=fadN {ECO:0000313|EMBL:AFK57393.1};
GN OrderedLocusNames=TMO_c0783 {ECO:0000313|EMBL:AFK57393.1};
OS Tistrella mobilis (strain KA081020-065).
OG Plasmid pTM3 {ECO:0000313|EMBL:AFK57393.1,
OG ECO:0000313|Proteomes:UP000005258}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC Geminicoccaceae; Tistrella.
OX NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK57393.1, ECO:0000313|Proteomes:UP000005258};
RN [1] {ECO:0000313|EMBL:AFK57393.1, ECO:0000313|Proteomes:UP000005258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA081020-065 {ECO:0000313|Proteomes:UP000005258};
RC PLASMID=Plasmid pTM3 {ECO:0000313|Proteomes:UP000005258};
RX PubMed=22458477; DOI=10.1021/ja301735a;
RA Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT agents.";
RL J. Am. Chem. Soc. 134:8625-8632(2012).
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}.
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DR EMBL; CP003239; AFK57393.1; -; Genomic_DNA.
DR RefSeq; WP_014748382.1; NC_017958.1.
DR AlphaFoldDB; I3TXA5; -.
DR KEGG; tmo:TMO_c0783; -.
DR PATRIC; fig|1110502.3.peg.5662; -.
DR HOGENOM; CLU_010448_0_0_5; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000005258; Plasmid pTM3.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR48075:SF7; 3-HYDROXYACYL-COA DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00725; 3HCDH; 2.
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 4: Predicted;
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; Plasmid {ECO:0000313|EMBL:AFK57393.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005258};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..777
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003680405"
FT DOMAIN 6..190
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 192..293
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 366..398
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 777 AA; 83403 MW; 1F6FBF1A9B44F0DE CRC64;
MTAIKKAAVI GAGVMGAGIA AHIANAGVPV VLLDIVPKGA ENRNALAEGA VQKMLKTKPK
SFMHPSRAKL VTTGNLEDDL GQLADVDWIV EAVIENLDIK RRLYATLDEV RKPGSIVSSN
TSTIPLGLLV EDRSAAFKGD FLITHFFNPP RYMRLLELVA GPETRPDAVE TIRAFGDHAL
GKGVVDCKDT PGFIANRIGT FWMQAAVTEA MDRKLDVEAV DALLSKPVGI PKTGVFGLID
LVGLDLMPHV AASMKATLPA DDAYHAIYRD SDLFRKMIAE GYTGRKGKGG FYRRRKDGGQ
TVQEALDLST GEYRAKRKPD LASIRAGAKD LRALVSHEDA GGAYAWAVIS AALSYTADLV
GVIADEVPAI DEAMRLGYGW KYGPFELIDR MGAGWFADRL TAEGRKVPEI LAAVAGNGTG
RFYRVSDGVL EFATRAGGYA PVPVPEGVLR LSDVKRRSKR VDGNGSASLW DLGDGVLCLE
FHTKMNAIDP GVLEMVAKST EIVRGGYKAL VVYNEADNFS VGANVGLALF ASNIAAWDMI
DGMIRMGQEA YKALKYAPFP VVGAPAGMAL GGGCEILLHC DAVQAHAETY MGLVEVGVGV
VPGWGGCKEL LFRWMANKRR PGGPMPAVGQ VFEMVSTAKV SESADEARDM LLLLDRDRIT
MNRDRVLADA KARALELAEG YQKPEAAEIS LPGPSARVAL EMAVDGFFQQ GKATPHDVVV
SGALARVLSG GDTDITETLR EDDVTRLERE AFISLLKTPA TLARIEHMLE TGKPLRN
//
