ID H6MYL7_GORPV Unreviewed; 478 AA.
AC H6MYL7;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Putative FAD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:AFA71895.1};
GN OrderedLocusNames=GPOL_c08280 {ECO:0000313|EMBL:AFA71895.1};
OS Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA71895.1, ECO:0000313|Proteomes:UP000009154};
RN [1] {ECO:0000313|EMBL:AFA71895.1, 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; AFA71895.1; -; Genomic_DNA.
DR RefSeq; WP_014358839.1; NC_016906.1.
DR AlphaFoldDB; H6MYL7; -.
DR STRING; 1112204.GPOL_c08280; -.
DR KEGG; gpo:GPOL_c08280; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_030705_1_2_11; -.
DR Proteomes; UP000009154; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR017224; Opine_Oxase_asu/HCN_bsu.
DR PANTHER; PTHR42949; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1.
DR PANTHER; PTHR42949:SF2; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PIRSF; PIRSF037495; Opine_OX_OoxA/HcnB; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000009154}.
FT DOMAIN 3..340
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT REGION 449..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 478 AA; 49797 MW; 2745005313D7DBBD CRC64;
MTHVAVIGAG PAGLAAAESA LHADATVTLV DLNDAPGGQY HRELPAAYRA ARPDVVGHEW
DAYRRRRDHV LGHPACTWMS NTVVFLLERR GAGPRSGRDA PRLHLLTGGV DAPDRTRAVL
EPDALILATG AHDRVLPFPG WTLPGVYTAG AAQTLARTER VALGRRAVIS GTGPFLLPVA
ESLSSVGTEV TEVLEANGIG TIARGWSAQP QRLLAQTGKA RDLMHYGRHL LAHRIPVRGG
QAVIRALGDS RVQGAVIARL DADWTPIPGT EREIEVDTIC VGHGFTPSLE LATAAGCAAV
EVAGGTFVGV DDNQLTSAPA VYAAGEVTGI GGAASAHAEG VVAGYAAAGR ADLITARMSR
ARVAAQHFST RLATAHPIGD GWQTWLEDTT VVCRCEATTL GQLRGAHSAE ESARATRLNT
RAGLGPCQAR FCGANVDAIC GRRAADRTGA SGLPAATPQN RPIAQPIRLG ELAGHDGR
//
