GenomeNet

Database: UniProt
Entry: H6MWG7_GORPV
LinkDB: H6MWG7_GORPV
Original site: H6MWG7_GORPV 
ID   H6MWG7_GORPV            Unreviewed;       273 AA.
AC   H6MWG7;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Enoyl-CoA hydratase domain-containing protein 3, mitochondrial {ECO:0000256|ARBA:ARBA00040545};
GN   OrderedLocusNames=GPOL_c31570 {ECO:0000313|EMBL:AFA74172.1};
OS   Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA74172.1, ECO:0000313|Proteomes:UP000009154};
RN   [1] {ECO:0000313|EMBL:AFA74172.1, ECO:0000313|Proteomes:UP000009154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44266 / VH2 {ECO:0000313|Proteomes:UP000009154};
RX   PubMed=22327575; DOI=10.1128/AEM.07969-11;
RA   Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D., Angelov A.,
RA   Liebl W., Daniel R., Steinbuchel A.;
RT   "Involvement of two latex-clearing proteins during rubber degradation and
RT   insights into the subsequent degradation pathway revealed by the genome
RT   sequence of Gordonia polyisoprenivorans strain VH2.";
RL   Appl. Environ. Microbiol. 78:2874-2887(2012).
CC   -!- FUNCTION: May play a role in fatty acid biosynthesis and insulin
CC       sensitivity. {ECO:0000256|ARBA:ARBA00037410}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000256|ARBA:ARBA00005254}.
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; CP003119; AFA74172.1; -; Genomic_DNA.
DR   RefSeq; WP_014360642.1; NC_016906.1.
DR   AlphaFoldDB; H6MWG7; -.
DR   STRING; 1112204.GPOL_c31570; -.
DR   KEGG; gpo:GPOL_c31570; -.
DR   eggNOG; COG1024; Bacteria.
DR   HOGENOM; CLU_009834_7_3_11; -.
DR   Proteomes; UP000009154; Chromosome.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
DR   CDD; cd06558; crotonase-like; 1.
DR   Gene3D; 1.10.12.10; Lyase 2-enoyl-coa Hydratase, Chain A, domain 2; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR   PANTHER; PTHR43602; -; 1.
DR   PANTHER; PTHR43602:SF1; ENOYL-COA HYDRATASE DOMAIN-CONTAINING PROTEIN 3, MITOCHONDRIAL; 1.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:AFA74172.1};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009154};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   273 AA;  28853 MW;  F665EF5422F9E82C CRC64;
     MTHTAQPATG VGTGSSDPDP VEVVVEAPLG IVTLTRPRRR NPLSTETMRA VTAALRTLGS
     DDAVRVVVIR AHGPAFSAGH DLSELVDRTL DDERAVFDTC VEMMAAVHEL DRPVIAEVAG
     AAFAAGCQLV ATCDLAVAAT TATFSTPGVR IGLFCSTPMV ALTRAIGRKR AMKMLLTGDA
     IDADTAADWG LVNDVVSPDE LATTVRELAL RIAGSSASTL AIGKRAFYQQ IDETETRAYE
     LMAETMATNA MTCDAQEGMS AFLAKRAPVW TDR
//
DBGET integrated database retrieval system