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Database: UniProt
Entry: A0A1Z1FBC9_9SPHN
LinkDB: A0A1Z1FBC9_9SPHN
Original site: A0A1Z1FBC9_9SPHN 
ID   A0A1Z1FBC9_9SPHN        Unreviewed;       678 AA.
AC   A0A1Z1FBC9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:ARU16075.1};
GN   ORFNames=A9D14_07560 {ECO:0000313|EMBL:ARU16075.1};
OS   Croceicoccus marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Croceicoccus.
OX   NCBI_TaxID=450378 {ECO:0000313|EMBL:ARU16075.1, ECO:0000313|Proteomes:UP000195807};
RN   [1] {ECO:0000313|EMBL:ARU16075.1, ECO:0000313|Proteomes:UP000195807}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E4A9 {ECO:0000313|EMBL:ARU16075.1,
RC   ECO:0000313|Proteomes:UP000195807};
RA   Wu Y.-H., Cheng H., Xu L., Huo Y.-Y., Wang C.-S., Xu X.-W.;
RT   "Complete genome sequence of esterase-producing bacterium Croceicoccus
RT   marinus E4A9.";
RL   Submitted (JAN-2017) 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: 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; CP019602; ARU16075.1; -; Genomic_DNA.
DR   RefSeq; WP_066844797.1; NZ_CP019602.1.
DR   AlphaFoldDB; A0A1Z1FBC9; -.
DR   STRING; 450378.GCA_001661675_01514; -.
DR   KEGG; cman:A9D14_07560; -.
DR   OrthoDB; 9771883at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000195807; 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; 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.
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:UP000195807}.
FT   DOMAIN          299..474
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          479..535
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   678 AA;  72051 MW;  6F3F86692E763918 CRC64;
     MGETVTVSVD NGIAIVTIAN PPVNALGRAV RQDLDAAADR IASDGDIRAA IIRADGGTFP
     AGADIAEFPD VPAPLHGDVF DKIEALHKPV VAAIHGTALG GGLELALACH FRVAAEGAKM
     GLPEVQLGLL PGARGTQRLP RLIGAEAALG MMLTGKPIDA AKALKAGLID ELVPATELDD
     KAFEMATALM AKDGPLPRAS QDSEWTRKDR DDPQLFDRVK DAHGRLFRGV IAPDAILTCV
     KAAVELPFDK GAEVEASEFA RLLSSDQSRA LIHVFFAMRE TAKVPGIGRE TPLIDIKSVG
     IIGAGTMGGG IAMCFANAGI PVKLVEVKAE ALERGLGVIR KNYENTAKKG RLTDDQVESL
     MNSIAGTLDM EDLSDVDLVI EAVFESMEIK EKVFTRLDSI AKQGAILASN TSFLDINHIA
     AMTSRPEMVL GLHFFSPANV MPLLEVVRGD KSSDSVIATG MKLGKTLRKT PVLAGVCDGF
     IANRLMFPYM VASQQMLLRG TPMQDIDAAM KQYGFAMGPI ALLDLIGLDV IDFPGEITMT
     GELVKAERRG QKLNGGFYDY DEKRRGTPAP AALEIIEKVR AAHGIETAPP LQADEILTGL
     LYPVVNEGAR ILEEGIALRA GDIDVTAILG YNWPSYQGGP MCWADIHGLD RIVSGLEKMD
     VQPAPLLAEK AASGGSFT
//
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