ID A0A0A6D0Z5_9SPHN Unreviewed; 676 AA.
AC A0A0A6D0Z5;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:KHA65546.1};
GN ORFNames=NI18_01165 {ECO:0000313|EMBL:KHA65546.1};
OS Sphingomonas sp. Ant20.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=104605 {ECO:0000313|EMBL:KHA65546.1, ECO:0000313|Proteomes:UP000033201};
RN [1] {ECO:0000313|EMBL:KHA65546.1, ECO:0000313|Proteomes:UP000033201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ant20 {ECO:0000313|EMBL:KHA65546.1,
RC ECO:0000313|Proteomes:UP000033201};
RA Ronca S., Frossard A., Guerrero L.D., Makhalanyane T.P., Aislabie J.M.,
RA Cowan D.A.;
RT "Draft Genome Sequence of Spingomonas sp. strain Ant20, isolated from oil-
RT polluted soil near Scott Base, Antarctica.";
RL Submitted (OCT-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 -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
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}.
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:KHA65546.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JRVI01000004; KHA65546.1; -; Genomic_DNA.
DR RefSeq; WP_037527504.1; NZ_JRVI01000004.1.
DR AlphaFoldDB; A0A0A6D0Z5; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000033201; Unassembled WGS sequence.
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:SF49; 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:UP000033201}.
FT DOMAIN 295..470
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 475..559
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 676 AA; 72416 MW; C043D5E869B80543 CRC64;
MTTPIRTERH DDVLVIISNN PPVNALGAAV RQGLEAAIKD GVADASITAM VIRCDGRTFF
AGADITEFGK PMVEPGLPTV VDMIEASSKP VVAAIHGTAL GGGCEVTLGC HYRVAVPSAK
IGTPEVKLGL LPGAGGTQRI PRIAGVKLAL EMTAKGDPIS AKKALDAGLI DKIVGEDSLE
ADAIAFAREI AAKRPLPRAS EKTAQADPDA VAAFKKENAR RFRNFDAPAA NIACVEKAAD
GSSFAEGVAF EREQFMALMM GVQSAAQRHI FFAERQAAKI DDVPADTKLR EIKRVGVIGA
GTMGGGIAMN FLSAGIPVTI VEMQQDALDR GTGVVRKNYE ATAAKGRMKP EQVEQAMGAL
KPTLDFADLA ECDLIIEAVY ETMEVKKDIF TKLDAIAKPG AILASNTSYL NIDEIAACTK
RPEDVVGMHF FSPANVMKLL EVVRGDKTAD DVLATVMALA KKIRKVAVVA GVTYGFIGNR
MLMPRQVEAT KLLLEGASPE QIDRVHVAFG MPMGPFQMSD LAGVDIGWHR DPSRIENIRD
ALAAENRWGQ KTKAGFYDYD EKRTPSNSPR VAEIIDDFRA KSGVTPREIS DEEIVARTLY
TMVNEGALIL EEGKAQRASD VDVVWIYGYG WPVYRGGPMF WAQSEGLPKV VAGLEKYGFP
VAKSLKDAAA SGGKIK
//