ID A0A0S8B329_9BACT Unreviewed; 711 AA.
AC A0A0S8B329;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KPK05590.1};
GN ORFNames=AMS20_06215 {ECO:0000313|EMBL:KPK05590.1};
OS Gemmatimonas sp. SG8_28.
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=1703357 {ECO:0000313|EMBL:KPK05590.1, ECO:0000313|Proteomes:UP000051120};
RN [1] {ECO:0000313|EMBL:KPK05590.1, ECO:0000313|Proteomes:UP000051120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_28 {ECO:0000313|EMBL:KPK05590.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPK05590.1}.
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DR EMBL; LJNQ01000085; KPK05590.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8B329; -.
DR PATRIC; fig|1703357.3.peg.3581; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000051120; Unassembled WGS sequence.
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; 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 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}.
FT DOMAIN 317..495
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 498..591
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 622..705
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 711 AA; 76320 MW; AFE7E990006D7188 CRC64;
MSTAALTVRI DRGVGWLELD VPGEAVNTIS PELRSDLAEA LESLARDGDV RAVVLVSRKP
GSFIAGADIN AFVALRGRDE AHALVRAGQA AINRVESLGK PVVAAIHGNC LGGGLELALA
CTYRIATDDP ATRIGLPEVQ LGIIPAAGGC QRLPRLIGLQ PALDMILAGK TIAASRARRL
GIVDELVHPC ILDQVAEQAA GRLADGWTPG RSRLSVRRLA TDRNPLGRRM LFTAARKQLL
KKTGGHYPAP MAALQAVEHG MTHGVEAGLD IEATLFAELA IGGVSRNLVR LFFATTALKK
DPGVQGDVPP PRPIAGIGVM GAGFMGAAIG GVAVLRAGTD VRFRDRDLRS VGGGLRVART
LLDEQLERRR ITTHAHRRLL SLLSGTDGWD GFGLTDLVIE AVYEDRDLKR QIFREVEAHV
RDDCVFASNT STIPISQIAD AVARPERVLG MHFFSPVAKM PLLEVIVAER TAPWATATAV
RYGRELGKTV IVVRDRPGFW VNRILAPYLN EAGRLLAEGV PVEVIDRAMM RFGFPVGPVT
LLDEVGLDVA HKGSEVLHEA FGARLQPTEG LVRMLDDGRL GRKNARGFYR YDDGKRREVD
LAAYEIIGAG ADPDVSKEDV QARLVFAMLN EAVLALDEGV VRSARDGDVG AVFGIGFPAF
RGGPLRYLDE LGLADAVDVL RDLQRTYGDR FAPAPRLVAM AGAGETFHPS S
//
