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Database: UniProt
Entry: H6MYN5_GORPV
LinkDB: H6MYN5_GORPV
Original site: H6MYN5_GORPV 
ID   H6MYN5_GORPV            Unreviewed;       430 AA.
AC   H6MYN5;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   SubName: Full=Putative ferredoxin--NAD(+) reductase {ECO:0000313|EMBL:AFA71913.1};
GN   OrderedLocusNames=GPOL_c08470 {ECO:0000313|EMBL:AFA71913.1};
OS   Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA71913.1, ECO:0000313|Proteomes:UP000009154};
RN   [1] {ECO:0000313|EMBL:AFA71913.1, 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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP003119; AFA71913.1; -; Genomic_DNA.
DR   RefSeq; WP_014358857.1; NC_016906.1.
DR   AlphaFoldDB; H6MYN5; -.
DR   STRING; 1112204.GPOL_c08470; -.
DR   KEGG; gpo:GPOL_c08470; -.
DR   eggNOG; COG0446; Bacteria.
DR   HOGENOM; CLU_003291_4_0_11; -.
DR   OMA; AAMRINQ; -.
DR   Proteomes; UP000009154; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR028202; Reductase_C.
DR   PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR   PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF14759; Reductase_C; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000009154}.
FT   DOMAIN          8..303
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          322..410
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   430 AA;  45611 MW;  CFB5CF62320C2005 CRC64;
     MADGAHGDVV LIGGGVASAA TADGLREEGF DGRIVLVADE PHLPYERPPL SKEFLSGEFT
     HGDFVARQQQ WYVDNDVELL LGTRVSALDP AAGTVTIADG GVLAYGAAVL ATGVRARTLP
     GFTGERVHVL RSMADSARLA EQLVPGRHVV IIGAGFIGCE VAAVAVQRGV RVSVFDPNPL
     PLRPLGEQVG TAMAGIHRSR GVELRTGEVI TSMTETLSGT VELRTGGGET VECDDVLIGI
     GSIPNAELAI DAGLDVDGGV LTDEFGRTSA PGVYAIGDVA ARWHPAHGRR VRVEHHDSAL
     RHGANLARTL TGSPVPFAEE PFFWTHQYEH NLQSVGRFAD TADGAGTTVL RGSVRDRSFS
     VFRLDDGQIT GMVAFDRPRD VLQARKVIGV PHRVTPDQLA DEGFALKSLL PQRTRTRSAS
     ARTARVEVAP
//
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