ID A0A1G1NYP9_9BACT Unreviewed; 711 AA.
AC A0A1G1NYP9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OGX34788.1};
GN ORFNames=A3C36_03995 {ECO:0000313|EMBL:OGX34788.1};
OS Omnitrophica WOR_2 bacterium RIFCSPHIGHO2_02_FULL_52_10.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1801858 {ECO:0000313|EMBL:OGX34788.1, ECO:0000313|Proteomes:UP000177305};
RN [1] {ECO:0000313|EMBL:OGX34788.1, ECO:0000313|Proteomes:UP000177305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(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}.
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:OGX34788.1}.
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DR EMBL; MHGR01000104; OGX34788.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1NYP9; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000177305; 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 318..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 620..705
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 711 AA; 78139 MW; 7ED5304577F008A0 CRC64;
MSLNFRIEND VGFIELDQED SKVNLLTSVM IRRLASILDE VAAHKDLCAL VIVSLKKDVF
IAGADIKEIE QITEAQDGTG KSRAGQDVLN KLEDLKIPTI AVIDGVALGG GCELALACTF
RLATFNEKVK IGLPEVNLGF IPGFGGTYRL PRVTGLAEGL KLILSGQPVD GEKALKIGLV
DRLITRENMH AQIYQFIADV HDRKIKRDKY NRKKAKGLEG LAKSSLILQF MIFRQSRQSV
LKLTKGFYPA PLRAVYVIKQ SFYMSRDKGL ALESRVFGEL AVTGISKNLV QVFYLSEKYK
KLTLEDAGDV RPAAITKAGV CGAGVMGGGI AQLLSYKGIW VRLKDVNYGA VAQGLKAAAK
LYGQLVERRK MKPAQAQKSM ARITGTLDYS GFAQADIIIE AVVEKMEVKK KVFGELGGVA
SPQAVLATNT SALSVTAMAE SIQDPSRVVG FHFFNPVHRM PLVEVITTKH TSKATVVTAL
QFAKTLGKTP IIVKDACGFL VNRILLGYIN EAGRILEECG QMERIDELVT RFGLPMGPFA
LSDEVGLDVG VKVLRILEEG LGERFKPVDT FEQIFAKGLL GKKSGKGFYY YGKDKVPNEE
DVRAILGRGP FSKFHSEDFL KRMMYIMINE AALCLHEGIV KEPGDVDVGM IFGTGFPPFR
GGLLRYADQT GIKRIVEDLK RFAGDLKAPR FEPCSLLREM GERNKNFYGT T
//
