ID G8PNR8_PSEUV Unreviewed; 717 AA.
AC G8PNR8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Fatty oxidation complex, alpha subunit {ECO:0000313|EMBL:AEV39560.1};
GN OrderedLocusNames=PSE_5058 {ECO:0000313|EMBL:AEV39560.1};
OS Pseudovibrio sp. (strain FO-BEG1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Stappiaceae; Pseudovibrio.
OX NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV39560.1, ECO:0000313|Proteomes:UP000005634};
RN [1] {ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile and symbiotically
RT interacting bacteria.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEV39560.1, ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV39560.1,
RC ECO:0000313|Proteomes:UP000005634};
RX PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile bacteria adapted
RT for symbiosis.";
RL Environ. Microbiol. 15:2095-2113(2013).
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}.
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; CP003147; AEV39560.1; -; Genomic_DNA.
DR RefSeq; WP_014287254.1; NC_016642.1.
DR AlphaFoldDB; G8PNR8; -.
DR STRING; 911045.PSE_5058; -.
DR KEGG; psf:PSE_5058; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_16_3_5; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000005634; 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}.
FT DOMAIN 301..477
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 482..575
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 611..696
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 717 AA; 76644 MW; 8F82BDFE31B99F32 CRC64;
MSSSFKSSGQ VSYELRGDVA VMTVSNAPVN ALSLAIRQDL VARIKQFEED EAAKAAVIVG
EDKVFIAGAD IREFKRPATE PHLPDVIDSI EACSKPVIAA IHGVALGGGL EVALGCHFRV
GVKGAKVGLP EVHLGIIPGA GGTQRLPRLA GYEKALEMIP SGAPIGADAA KSAGILDGVS
DEADAVAAGL AFARSVIDNG TPLRRCSELV APAVDAQVFV DAKAAVAKRA RGQKSPVVCV
EAIEVASQTS FVDGMAKERE MFMELKNSAQ HRALSHAFFA DRALGKLPEI EGIAPRMLKS
IGVIGGGTMG AGIATGALMN GLSVTLIERD DDALGRAKAT IAKNVGGAVK KGKLSADQEQ
RIFAEALSLS TDYASLSELD LVVEAVFEDI DVKKQVFEKL DEVCKEGAVL ATNTSYLDVN
AIAAVTKRPQ DVIGLHFFSP AHIMKLLEVV VADKTAPDVI ATGFLLGKIM RKVAVRAGVC
DGFIGNRILA TYRAAADAIV VDGSTPFEVD EVMLEFGFPM GPYAVADLAG LDIGWATRKH
KAPTRDPRER YFTFADRMCE QGWFGQKTSK GYYVYEDGAR KGTPNPAVLD ILTEERKEKR
INAKKLTKTQ ILDRYMAAMV NEAAKVVEDG IALRPLDVDM TLIYGYGFPR WRGGPMQYAD
EIGLEKILSN IKAYAEEDAY FWQPAKLLEE LVASGRTFAD LNAESGNNSA AKKHENA
//
