ID H6MVZ2_GORPV Unreviewed; 339 AA.
AC H6MVZ2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Putative hydrolase/esterase/lipase {ECO:0000313|EMBL:AFA71687.1};
GN OrderedLocusNames=GPOL_c06180 {ECO:0000313|EMBL:AFA71687.1};
OS Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA71687.1, ECO:0000313|Proteomes:UP000009154};
RN [1] {ECO:0000313|EMBL:AFA71687.1, 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).
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DR EMBL; CP003119; AFA71687.1; -; Genomic_DNA.
DR AlphaFoldDB; H6MVZ2; -.
DR STRING; 1112204.GPOL_c06180; -.
DR KEGG; gpo:GPOL_c06180; -.
DR eggNOG; COG0657; Bacteria.
DR HOGENOM; CLU_012494_13_0_11; -.
DR Proteomes; UP000009154; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR PANTHER; PTHR48081:SF8; STERYL ACETYL HYDROLASE MUG81-RELATED; 1.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:AFA71687.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009154}.
FT DOMAIN 101..299
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT ACT_SITE 174
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10038"
SQ SEQUENCE 339 AA; 36876 MW; 971EBBBED9A5B82A CRC64;
MPHRTRPTPA QEVFGMPIVQ HRKASALSYP IWVGSRLFLK PLLSLWPLNR EGMAGLFLID
RMFAVGPKPH NVVREQIRLG DRPAEVILPT GPSRRDSDTA ILYLHGGAFV VGGVGTHRSI
AARLSRACEV PVFSLVYRQL PAAGVGTSVS DAMSAYRELL TERGYRRVVV AGDSAGGFLA
AKVVEGAAAQ GLPAPAALIG FSPLLDLDLA DNPDRSSRSD AYIPLSQLVK LAPHFLRGPV
AFTGVRRIAD LELEDFPPTI MITAENELLE PDVIDLVENL DEAGVRAEAH SYSWQIHAFP
VFGSHHRETL EAIEVSAEFA GRAIREAKSA DDRENKWAG
//
