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Database: UniProt
Entry: D1A473_THECD
LinkDB: D1A473_THECD
Original site: D1A473_THECD 
ID   D1A473_THECD            Unreviewed;       418 AA.
AC   D1A473;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Geranylgeranyl reductase {ECO:0000313|EMBL:ACY99947.1};
GN   OrderedLocusNames=Tcur_4420 {ECO:0000313|EMBL:ACY99947.1};
OS   Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC
OS   9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Thermomonospora.
OX   NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY99947.1, ECO:0000313|Proteomes:UP000001918};
RN   [1] {ECO:0000313|EMBL:ACY99947.1, ECO:0000313|Proteomes:UP000001918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 /
RC   NCIMB 10081 / Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX   PubMed=21475583; DOI=10.4056/sigs.1453580;
RA   Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA   Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Brettin T., Han C., Detter J.C., Rohde M., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL   Stand. Genomic Sci. 1:13-22(2011).
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DR   EMBL; CP001738; ACY99947.1; -; Genomic_DNA.
DR   RefSeq; WP_012854730.1; NC_013510.1.
DR   AlphaFoldDB; D1A473; -.
DR   STRING; 471852.Tcur_4420; -.
DR   KEGG; tcu:Tcur_4420; -.
DR   eggNOG; COG0644; Bacteria.
DR   HOGENOM; CLU_024648_5_2_11; -.
DR   OrthoDB; 9795712at2; -.
DR   Proteomes; UP000001918; Chromosome.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR011777; Geranylgeranyl_Rdtase_fam.
DR   NCBIfam; TIGR02032; GG-red-SF; 1.
DR   PANTHER; PTHR42685; GERANYLGERANYL DIPHOSPHATE REDUCTASE; 1.
DR   PANTHER; PTHR42685:SF4; GERANYLGERANYL DIPHOSPHATE REDUCTASE, CHLOROPLASTIC; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001918}.
FT   DOMAIN          8..316
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   418 AA;  45707 MW;  66711D69D89AADCB CRC64;
     MTESSGRADA IVVGAGPAGS STAYWLAQAG LDVLLLEKAT FPRDKICGDG LTPRAVRALI
     SMGVDLDAPG WARTRGLRIY GGGVKIELDW PELASFPDFG LVRARTDLDR LLAEHAAKAG
     ARLQQGCNVT GPIVDERTGR IVGVTAKYQG QEVSYRAPLV VAADGNSSRL SLAMGLRRRT
     DRPMGVAVRR YYRTPRHDDE YLESWLELWD GQRLLPGYGW VFPLGNGLSN VGLGLLNTSK
     AFQNVDYRAM LRKWTAGMPE EWQIDEDHAT GPIRGAALPM GFNRQPHYTR GLLLVGDAGG
     MINPFNGEGI DYGLESGKLA AETIVQALAR STPGRRERTL HQYPRILKEQ HGGYFTLGRI
     FVQAIGDPRV MKFLTRHGLP HPTLMRFTLK LLANLTDPRG GDAMDRVINA LKKAAPAA
//
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