ID A0A143BM88_9BACT Unreviewed; 770 AA.
AC A0A143BM88;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:AMW05675.1};
GN ORFNames=GEMMAAP_14435 {ECO:0000313|EMBL:AMW05675.1};
OS Gemmatimonas phototrophica.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=1379270 {ECO:0000313|EMBL:AMW05675.1, ECO:0000313|Proteomes:UP000076404};
RN [1] {ECO:0000313|EMBL:AMW05675.1, ECO:0000313|Proteomes:UP000076404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP64 {ECO:0000313|EMBL:AMW05675.1,
RC ECO:0000313|Proteomes:UP000076404};
RX PubMed=24821787; DOI=10.1073/pnas.1400295111;
RA Zeng Y., Feng F., Medova H., Dean J., Koblizek M.;
RT "Functional type 2 photosynthetic reaction centers found in the rare
RT bacterial phylum Gemmatimonadetes.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:7795-7800(2014).
RN [2] {ECO:0000313|EMBL:AMW05675.1, ECO:0000313|Proteomes:UP000076404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP64 {ECO:0000313|EMBL:AMW05675.1,
RC ECO:0000313|Proteomes:UP000076404};
RX PubMed=26636755; DOI=10.1111/1758-2229.12363;
RA Zeng Y., Baumbach J., Barbosa E.G., Azevedo V., Zhang C., Koblizek M.;
RT "Metagenomic evidence for the presence of phototrophic Gemmatimonadetes
RT bacteria in diverse environments.";
RL Environ. Microbiol. Rep. 8:139-149(2016).
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; CP011454; AMW05675.1; -; Genomic_DNA.
DR RefSeq; WP_026848611.1; NZ_CP011454.1.
DR AlphaFoldDB; A0A143BM88; -.
DR STRING; 1379270.GEMMAAP_14435; -.
DR GeneID; 78445317; -.
DR KEGG; gph:GEMMAAP_14435; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR OrthoDB; 9815331at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000076404; Chromosome.
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; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000076404};
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_5007506877"
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; 82730 MW; A744344310F46CE8 CRC64;
MRVTTVGVVG AGAMGSGIAA LAASAGCRVV LLDIPGDADP ASPNRSAPAK NGLAKAIKSK
PASFMEAAAV ARVRVGNTDD HVSWLAECDW ICEAIIELAE PKQQLFARIE ALMKPTAIVS
SNTSGIPMAT LLEGRSEKFR RRFLGTHFFN PPRYMHLLEV IPTPETDPAV IGAMNGFAER
TLGKGIVIAK DVPGFIANRL GVYGMVATMR RMQQHGLTID EVDGLTGSLI GRARSATFRT
GDLSGLDVLA HVTKGIGAAT GEDFALPTWV HEALVGTGKL GDKTGGGFYS KTKTGTLTFD
WKTTSYVPQQ RLEGGDIRQA IRLPIAQRLP VIKTLPGAQG AFVRDHVVDA AHYTLTLASQ
LAHDIVAIDR AMEWGYGWEA GPFQVMDALG IDWLREQFKA EGLDVPPLLE LAQGSFYKNG
EYLTFDGQYE PLPAIPGRIS LAGLAQSGRV LEDNGLSRLI DLGDGVACFE FRSKMNSLGQ
GVLEGLEKSL RKVEKLGFNG LVIGNEDPRA FSVGADLSLV SFAVSAGAWD DIEASIRTFQ
DAVMSIRRAP FPVVVAPAGM TLGGGCEFTL HADAVQAHAE TYMGLVEVGV GLLPGGGGTK
ELLMRFTSEL QNYEEVDLFA AVKRAFKLIA FATTTTSAFE GRAFGFLRDR DRISMNRDHQ
LSDAKQRVLD LAPGYLPPIE RTVRALGREG IGNLEYALWA AKEGGQASAH DVRVGRAVAY
VLCGGDGSPR DVTEQDLLDL EREQFLSLLG TKETQERIAY TLKTGKPLRN
//
