ID A0A1A0FMQ5_9GAMM Unreviewed; 700 AA.
AC A0A1A0FMQ5;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:OBA00762.1};
GN ORFNames=ADS46_00125 {ECO:0000313|EMBL:OBA00762.1};
OS Halomonas sp. G11.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1684425 {ECO:0000313|EMBL:OBA00762.1, ECO:0000313|Proteomes:UP000092250};
RN [1] {ECO:0000313|EMBL:OBA00762.1, ECO:0000313|Proteomes:UP000092250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G11 {ECO:0000313|EMBL:OBA00762.1,
RC ECO:0000313|Proteomes:UP000092250};
RA Naifar M., Chouchane H., Najjari A., El Hidri D., Mahjoubi M., Ghedira K.,
RA Soufi L., Salah A., Raddadi N., Sghaier H., Ouzari H.I.,
RA Eddine Masmoudi A.S., Cherif A.;
RT "Genomic basis for crude oil degradation, heavy metal resistance and high
RT salt tolerance of Halomonas hydrocarbonoclasticus G11 isolated from
RT Tunisian Chott El-Djerid salt lake.";
RL Submitted (FEB-2016) 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 -!- 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:OBA00762.1}.
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DR EMBL; LYXG01000001; OBA00762.1; -; Genomic_DNA.
DR RefSeq; WP_066314641.1; NZ_LYXG01000001.1.
DR AlphaFoldDB; A0A1A0FMQ5; -.
DR OrthoDB; 5389341at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000092250; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-KW.
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; 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.
PE 4: Predicted;
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140}.
FT DOMAIN 307..484
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 487..579
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 700 AA; 75435 MW; 790082315F7805B8 CRC64;
MVETSTAGRV HLDQDGAVAI ITLDNPPVNS SNDAVRRGIL AALDKIDTQQ SRAVVLMGKG
PHLMAGANLR ELAHEPTEPT LPQVTAALSA FPIPVIAVIS GHTLGGGLEL ALACDSRITT
PTALLGLPEV TVGVIPGAGG TQRLPRAVGL PKALEMIISG KPITAVEAYE VGLVDELLNT
TQGETSGGEA PEAEVLKAIL AYANRYQGGK QPLAECDVPP VDKQALQARI TKLLARARGL
PSAPVAAEVV MKATTLSFSA AIAEERAQFL ALRGSEPAQA LRYLFFAERE KPFEPTHPVK
AAPVSRISVV GAGTMGSGIA LCALKAGYSV DLLELNDQAL EAGVTRITQA LDEGVKRQRL
TQAQRHDALS RLKPTQQLPE VAGTDLVIEA IVEELAIKRS LFADLAQWVS ESTLLASNTS
YLDIEQIAEG IPHPERVLGL HFFSPADRMP LMEIVRCKAT SEQSLITAVS VARRLKKKAI
VVANAWGFVG NRLYAAYRRQ CEFMLEEGAS PEQIDTALEA YGFAMGPFKV ADMSGLDIAL
KMRQQTADTR HLRRYVGVPD LLCEAGRFGR KTGRGYYRYD EAMQPASDPE VAQLVERYRE
EHAITPKAFS AQEIQQRAEL ALINEALLLL EEGVCQRPAD IDIALVNGYG FPRWRGGPLF
IARQMSSNEL AKALDKLAEV SGKGHQRANL QSLNVQNSEE
//
