ID A0A087NDM7_9SPHN Unreviewed; 722 AA.
AC A0A087NDM7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:KFL47230.1};
GN ORFNames=IL54_2653 {ECO:0000313|EMBL:KFL47230.1};
OS Sphingobium sp. ba1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1522072 {ECO:0000313|EMBL:KFL47230.1, ECO:0000313|Proteomes:UP000029094};
RN [1] {ECO:0000313|EMBL:KFL47230.1, ECO:0000313|Proteomes:UP000029094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ba1 {ECO:0000313|Proteomes:UP000029094};
RA Manzari C., Chiara M., Costanza A., Leoni C., Picardi E., Trotta M.,
RA Volpicella M., D'Erchia A.M., Horner D.S., Pesole G., Ceci L.R.;
RT "Draft genome sequence of a Kanamycin and Nickel resistant bacterium
RT Sphingobium species.";
RL Submitted (JUL-2014) 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}.
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:KFL47230.1}.
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DR EMBL; JPPQ01000069; KFL47230.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087NDM7; -.
DR PATRIC; fig|1522072.3.peg.1341; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000029094; 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 315..493
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 496..593
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 722 AA; 77352 MW; FE2E2BC4C08F1783 CRC64;
MKTMQLQKAD DGFAILTLDA EGSMNVVNDA FLADMEAVTK QIAEDDSITG VILTSAKASF
MAGADLKQLV NGFGTLTASQ AYAFSKRATD MHRAIEQSGK PWVAAINGLA LGGGFELTLA
CHRRILVDDA KVQVGLPEVN VGLLPGSGGT VRLGLIAGMK TALDLLLSGR SVGPAEALKL
KIVDEVVSAD TLIDAAKAWL ATAPDPVKPW DVKGWTPPQK KGLTVPEDST AYMMATGGIA
KVGYNQPAPL AILNCVFQGL QLPFDKALTV EGKYFAKLLT DPVARNIIRT TFISKQAAEK
GARRPEGFEK FAAKKVGVLG AGMMGAGIAY VSANAGIEVI LIDRDTATAQ KGKDYAARVL
GKLIEKGKTT QDKADAVLAR ITPTDDFALL DGCDLVVEAV FEDTGIKAET TRKAEAVLPD
HAVFASNTST LPISQLAQAS QRPDQFIGLH FFSPVERMGL VEVIMGKQTS KATLAKGLDY
IAQLRKTPIV VNDSRGFYTS RVFQMLIHEG AAMLAEGVPP AVIENAAKAV GMPVGPLALL
DELTLDLPLK IVDQAIAEEG DAYTPPAGVA VMRRMKDEIG RSSRKAGGAF YDYPEGGKKH
LWKGLADHFP TKADWDIEEL KQRYLYAQAM ETARCLEENV LETPQDADLG AIYGWGFPAW
TGGTISYIDT IGIKTFVQES DRLAQLYGPR FLPSAWLRDK AARGEDFYTP ASETTVKEPV
PA
//
