ID A0A1Q7QJ82_9CHLR Unreviewed; 698 AA.
AC A0A1Q7QJ82;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OLD51815.1};
GN ORFNames=AUI58_05835 {ECO:0000313|EMBL:OLD51815.1};
OS Chloroflexi bacterium 13_1_40CM_2_70_6.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1805070 {ECO:0000313|EMBL:OLD51815.1, ECO:0000313|Proteomes:UP000185765};
RN [1] {ECO:0000313|EMBL:OLD51815.1, ECO:0000313|Proteomes:UP000185765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(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:OLD51815.1}.
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DR EMBL; MNHK01000078; OLD51815.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7QJ82; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000185765; 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; 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.
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 316..493
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 496..587
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 698 AA; 72744 MW; DD4D325C08290E29 CRC64;
MPSAQVRSVT FVPADDSGVA RIVIDRPDDP VNAMDLRVVE DFAAAIVAAR AAAPRGLIVA
SGKDGRFVAG ADLSLLSGGS RIEIERAIRA FQQVLNDLAA LPFTTVAAIN GAAIGGGLEL
ALACDRRIIA DAPSARVGLT ETRLGLVPGA GGTQRLPRLI GLVRALDVIL NARTLAPRRA
LRAGIVDEVV HPAVLLKAAA DHALRDRKQK PRGGATAVER ATTWLPPVRA FALRQARSRV
LAETKGRYPA PLAAIDAIAT GLAKGMAAGL DAEARALGEL AVGGTGKNLV ALALLTLHQR
KAVLQGLGRA RPIAAVGVVG LGFMGSGIAQ AAAAGGLRVR ARDRDAAAVA KGLSTIRQLT
AEAAKKGVFE RREAARIVGR ITGGPDLAGF SGADLVIEAV FEELATKQRV VEELEQVLRP
DAVIASNTSA LPIAEIARRA RAPERVVGMH FFSPVHRMPL IEVVRSARAD PDAIATAVAA
AHALGKTAIV VGDGAGFYTT RVLSVMIGEA FAMLAEGADI EAIDRAMVEF GWPVGPLQEV
DEVGLEVAAH AGETVAKARG ITPPTIVNAL VAEGFKGKAK GGGFYRYSGG RRTPNPRVRE
LVGVDSRPVV EDIAERLTLA LVNEAARCLD ERVLRSPAEG DLGAVLGFGF PPFLGGPFRY
ADALGDGVVA SLERLAAAHG DRFAPANALR SRRPFFRV
//
