ID A7HUI1_PARL1 Unreviewed; 692 AA.
AC A7HUI1;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase NAD-binding {ECO:0000313|EMBL:ABS63564.1};
GN OrderedLocusNames=Plav_1949 {ECO:0000313|EMBL:ABS63564.1};
OS Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Parvibaculaceae; Parvibaculum.
OX NCBI_TaxID=402881 {ECO:0000313|EMBL:ABS63564.1, ECO:0000313|Proteomes:UP000006377};
RN [1] {ECO:0000313|EMBL:ABS63564.1, ECO:0000313|Proteomes:UP000006377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-1 / DSM 13023 / NCIMB 13966
RC {ECO:0000313|Proteomes:UP000006377};
RX PubMed=22675581; DOI=10.4056/sigs.2215005;
RA Schleheck D., Weiss M., Pitluck S., Bruce D., Land M.L., Han S.,
RA Saunders E., Tapia R., Detter C., Brettin T., Han J., Woyke T., Goodwin L.,
RA Pennacchio L., Nolan M., Cook A.M., Kjelleberg S., Thomas T.;
RT "Complete genome sequence of Parvibaculum lavamentivorans type strain (DS-
RT 1(T)).";
RL Stand. Genomic Sci. 5:298-310(2011).
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: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000256|RuleBase:RU003707}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC hydratase/isomerase family. {ECO:0000256|ARBA:ARBA00008750}.
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DR EMBL; CP000774; ABS63564.1; -; Genomic_DNA.
DR AlphaFoldDB; A7HUI1; -.
DR STRING; 402881.Plav_1949; -.
DR KEGG; pla:Plav_1949; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_16_3_5; -.
DR OrthoDB; 9771883at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000006377; Chromosome.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23309; 3-HYDROXYACYL-COA DEHYROGENASE; 1.
DR PANTHER; PTHR23309:SF9; PEROXISOMAL BIFUNCTIONAL ENZYME; 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.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000006377}.
FT DOMAIN 302..478
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 483..567
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 602..687
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 692 AA; 75038 MW; E2A5781A6E0D0FFE CRC64;
MTAINDVTTL ETVGEVAVLT LNSPPVNALS APVREGINNG IKQAMENDAV KAIVLICEGK
TFIAGADITE FGKAPAGPSL FDALNMIEFA SKPVIAAIHG TALGGGLEVA LTCHYRVAVP
SAKCGLPEVN LGLLPGAGGT QRLPRIVGPE KALEMVTSGS HVGAKKCLEM GLVDELTEEG
KLRDGAIAFA KKIVAEKRPL KRVRDLSDKV EAARGKPEIF SEFRKANARK FRGFLAPEYN
IQCIEAAVNL PFDEGIKVEQ KLFRELVTGT QSAAQRHVFF AERQVWKLPD VPADTPTIPV
NKVGIIGAGT MGGGIAMNFL NVGLPVTIVE TKQEALDRGI ATIRKNYENS AKKGRFSMEE
VEKRMGLLTG SLEMEALADS DLVIEAVFEN MDVKKQVFSK LDAIVKQGAI LATNTSALNI
DEIATAVKRP EAVIGLHFFS PANVMRLLEV VRADKTSKPV IATSMQLAKK IGKIAALVGV
CPGFVGNRIL AQRQREAQKL ILEGAMPWDV DRVLYDFGLP MGPFAMSDLA GLDIGWSKEK
SQGATIRDVL CEMDRRGQKT GAGFYDYDEN RNAKPSPVVE KIILDFAQKK GINRRKISDD
EILERCIYPM INEGAKILEE GKAIRSSDID IVWINGYGFP VYRGGPMFYG DTVGADKVLA
KMKEFQAQMG DDFKPAALLE KIVAEGKKFS DF
//
