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Database: UniProt
Entry: H5XSK3_9FIRM
LinkDB: H5XSK3_9FIRM
Original site: H5XSK3_9FIRM 
ID   H5XSK3_9FIRM            Unreviewed;       282 AA.
AC   H5XSK3;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=2-polyprenylphenol hydroxylase-like oxidoreductase {ECO:0000313|EMBL:EHQ88103.1};
GN   ORFNames=DesyoDRAFT_0931 {ECO:0000313|EMBL:EHQ88103.1};
OS   Desulfosporosinus youngiae DSM 17734.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=768710 {ECO:0000313|EMBL:EHQ88103.1, ECO:0000313|Proteomes:UP000005104};
RN   [1] {ECO:0000313|EMBL:EHQ88103.1, ECO:0000313|Proteomes:UP000005104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17734 {ECO:0000313|EMBL:EHQ88103.1,
RC   ECO:0000313|Proteomes:UP000005104};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Lu M., Land M.L., Hauser L., Pester M.,
RA   Spring S., Ollivier B., Rattei T., Klenk H.-P., Wagner M., Loy A.,
RA   Woyke T.J.;
RT   "The Noncontiguous Finished genome of Desulfosporosinus youngiae DSM
RT   17734.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR006816-1};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR006816-1};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|PIRSR:PIRSR006816-2};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit.
CC       {ECO:0000256|PIRSR:PIRSR006816-2};
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DR   EMBL; CM001441; EHQ88103.1; -; Genomic_DNA.
DR   RefSeq; WP_007780019.1; NZ_CM001441.1.
DR   AlphaFoldDB; H5XSK3; -.
DR   STRING; 768710.DesyoDRAFT_0931; -.
DR   eggNOG; COG0543; Bacteria.
DR   HOGENOM; CLU_003827_1_0_9; -.
DR   OrthoDB; 9778346at2; -.
DR   Proteomes; UP000005104; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:InterPro.
DR   CDD; cd06219; DHOD_e_trans_like1; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR012165; Cyt_c3_hydrogenase_gsu.
DR   InterPro; IPR019480; Dihydroorotate_DH_Fe-S-bd.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR43513; DIHYDROOROTATE DEHYDROGENASE B (NAD(+)), ELECTRON TRANSFER SUBUNIT; 1.
DR   PANTHER; PTHR43513:SF3; DIHYDROOROTATE DEHYDROGENASE B (NAD(+)), ELECTRON TRANSFER SUBUNIT-RELATED; 1.
DR   Pfam; PF10418; DHODB_Fe-S_bind; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PIRSF; PIRSF006816; Cyc3_hyd_g; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|PIRSR:PIRSR006816-2};
KW   FAD {ECO:0000256|PIRSR:PIRSR006816-1};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR006816-1};
KW   Iron {ECO:0000256|PIRSR:PIRSR006816-2};
KW   Iron-sulfur {ECO:0000256|PIRSR:PIRSR006816-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR006816-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005104};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..282
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003602247"
FT   DOMAIN          1..95
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   BINDING         62..64
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-1"
FT   BINDING         222
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         225
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         237
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
SQ   SEQUENCE   282 AA;  30124 MW;  F762D996C15E41FA CRC64;
     MYHVVKKRLL ATGIALLDVN APAVAAKVEP GQFVIVRVDE LSERIPLTVM DFDREKGTIT
     IVVQDVGYSS AIITRMNEGD QFQDFVGPLG VASEVENYGT VVCIGGGLGI APVHPIARAL
     KEAGNHVISV LGSRSADLLI LEDEMHAASS EVVIATNDGS KGVKGFVTDG LAEVLAQGHQ
     VKAIWAIGPM IMMKAVVDYT RPLGIKTIVS MNPIMVDGTG MCGACRISVG DETKFACVDG
     PEFDGHLVDF DLAMKRLAFY KDEENQAKAR LECDCGKEGG HH
//
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