ID Q0C4E2_HYPNA Unreviewed; 743 AA.
AC Q0C4E2;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE SubName: Full=Enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase/3-hydroxybutyryl-CoA epimerase {ECO:0000313|EMBL:ABI75436.1};
DE EC=1.1.1.35 {ECO:0000313|EMBL:ABI75436.1};
DE EC=4.2.1.17 {ECO:0000313|EMBL:ABI75436.1};
DE EC=5.1.2.3 {ECO:0000313|EMBL:ABI75436.1};
GN OrderedLocusNames=HNE_0672 {ECO:0000313|EMBL:ABI75436.1};
OS Hyphomonas neptunium (strain ATCC 15444).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales;
OC Hyphomonadaceae; Hyphomonas.
OX NCBI_TaxID=228405 {ECO:0000313|EMBL:ABI75436.1, ECO:0000313|Proteomes:UP000001959};
RN [1] {ECO:0000313|EMBL:ABI75436.1, ECO:0000313|Proteomes:UP000001959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15444 {ECO:0000313|EMBL:ABI75436.1,
RC ECO:0000313|Proteomes:UP000001959};
RX PubMed=16980487; DOI=10.1128/JB.00111-06;
RA Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G.,
RA Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D.,
RA Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R.,
RA Brinkac L.M., Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G.,
RA Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N.,
RA Ward N.L.;
RT "Comparative genomic evidence for a close relationship between the
RT dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
RT crescentus.";
RL J. Bacteriol. 188:6841-6850(2006).
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}.
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DR EMBL; CP000158; ABI75436.1; -; Genomic_DNA.
DR RefSeq; WP_011645701.1; NC_008358.1.
DR AlphaFoldDB; Q0C4E2; -.
DR STRING; 228405.HNE_0672; -.
DR KEGG; hne:HNE_0672; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_16_3_5; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000001959; Chromosome.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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 Isomerase {ECO:0000313|EMBL:ABI75436.1};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ABI75436.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000313|EMBL:ABI75436.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001959}.
FT DOMAIN 331..509
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 512..609
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 743 AA; 80251 MW; 5578E8E27C526A96 CRC64;
MKLETFKFDI DADGIAHAIF DVPGRSMNTL TGKAVQDIIA ITQEVASNEK ITGLVISSGK
ESGFCAGADL GEMGNRAGAG GEQKKKSEDE LKKEQFEAGF ALNGTLRKLE TCGKPVAVAL
NGLALGGGLE VALACHYRVA ANDNPRIQFG LPEAKIGLLP GAGGTQRLPR LVGVQAALPL
ILQGESFNAE KAHSMGVVQE LAPGAETVAR AKAWVKANPK AKAPWDEKGY KVPGGVPHKS
PGAGQVATMA NMMLASKTYG NYPAQKNILS CIYEGIQVPI DAGLRIETRY FINTQQRPEA
KAMIRSLFLS TQALSKGANR PSGFEKAELK KVGIIGAGLM GAGIAYEQAR AGIRTVLVDV
KQEAAEKGKQ YAVRLVEKDI SRGKSTKEKG DALLSLITPT TDYKLLEDCD LIVEAVYEDI
DLKHKVLADA EAALGENAIV GSNTSTLPIT QLSTPLKRKD KFIGIHFFSP VERMGLVEII
MGKETSQETL AKTIDYVLKI RKTPIVVNDS RGFYTSRCFG TYTQEGLEML SEGIKPAIIE
NVGRQAGMPM GPLEVSDSVG LDTALKVGRA TAKAVGFDYN EAPLGRMMAW IVEDKGRVGR
KAGKGFYDYN DQGKPDRIWP DLNEQVEVKI DECPPALKKE LTNRLLIRQA IEVSRCFEEG
VIQDARDGDI GSILAWGFAP YTGGCVSYMD LIWGVPAFVA EADRLAEKYG ERFRPGKLLR
EMAEKGQSFY ERFPPAGEKK AAA
//
