ID C1AAJ9_GEMAT Unreviewed; 770 AA.
AC C1AAJ9;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase {ECO:0000313|EMBL:BAH39797.1};
DE EC=4.2.1.- {ECO:0000313|EMBL:BAH39797.1};
GN OrderedLocusNames=GAU_2755 {ECO:0000313|EMBL:BAH39797.1};
OS Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC
OS 100505).
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=379066 {ECO:0000313|EMBL:BAH39797.1, ECO:0000313|Proteomes:UP000002209};
RN [1] {ECO:0000313|Proteomes:UP000002209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-27 / DSM 14586 / JCM 11422 / NBRC 100505
RC {ECO:0000313|Proteomes:UP000002209};
RA Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y., Oguchi A.,
RA Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S., Yokoyama H.,
RA Tanikawa S., Hanada S., Kamagata Y., Fujita N.;
RT "Complete genome sequence of Gemmatimonas aurantiaca T-27 that represents a
RT novel phylum Gemmatimonadetes.";
RL Submitted (MAR-2006) 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}.
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DR EMBL; AP009153; BAH39797.1; -; Genomic_DNA.
DR RefSeq; WP_015894566.1; NC_012489.1.
DR AlphaFoldDB; C1AAJ9; -.
DR STRING; 379066.GAU_2755; -.
DR KEGG; gau:GAU_2755; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_010448_0_0_0; -.
DR OrthoDB; 9815331at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000002209; 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; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR48075:SF7; 3-HYDROXYACYL-COA DEHYDROGENASE-RELATED; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Lyase {ECO:0000313|EMBL:BAH39797.1}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000002209};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..770
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002906670"
FT DOMAIN 5..191
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 194..290
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 770 AA; 82437 MW; 5C49551E8D1E5818 CRC64;
MRVTTVGVVG AGAMGSGIAA LAASAGCRVV LLDIPGDTDP TSPNRSAPAR NGLQKAIKSK
PASFMETAAA ARVRTGNTED HLAWLAECDW ICEAIIEQPA PKQQLFTRIE ALMKPTAIVS
SNTSGIPMAV LLEGRSEKFR RRFLGTHFFN PPRYMHLLEI IPTPETDPAV IGAMREFAER
TLGKGIVIAK DVPGFIANRL GVYGMVATMR RMQEHGLTID EVDGLTGSLI GRARTATFRT
GDLSGLDVLA HVTKGIGAAT GEDFALPGWM LTDLVATGKL GDKTGGGFYQ KTKTGTLTYD
WKTSQYVPQQ RLEGGDIGQA IRLPIAQRLP AAKAVPGAQG AFLRDHLVDA AHYTLTLASQ
LGYDLVAIDR AMEWGYGWEA GPFQVMDALG LDWLREEFRA HGLDIPALLD LAQGSFYKNG
EYLTFEGTYE PVPAIPGRIS LAGLAQSGRV LEDNGLSRLI DLGDGVACFE FRSKMNSLGA
GVLEGLEKSL RKIEKLGFNG LVIGNEDARA FSVGADLSLV SFAISAGAWD DIAVSCKAFQ
DAVMSIRRAP FPVVVAPAGM TLGGGAEFTL HADAVQAHAE TYMGLVEAGV GLIPGGGGTK
ELLVRFTGEL QQYEEVDLFA AVKRAFKLIA FATTSTSAPE AKALGFLSSR DRISMNRDHQ
IADAKRRVLD LAPGYLPPIE RTVRALGREG LGNLEYALWA AKEAGQASAH DVRVGRAAAY
VLCGGDGAAR DVTEQDLLDL EREQFMSLLG TKETQERIAY TLKTGKPLRN
//
