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Database: UniProt
Entry: E4RL58_HALHG
LinkDB: E4RL58_HALHG
Original site: E4RL58_HALHG 
ID   E4RL58_HALHG            Unreviewed;       276 AA.
AC   E4RL58;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   SubName: Full=Oxidoreductase FAD/NAD(P)-binding domain protein {ECO:0000313|EMBL:ADQ14822.1};
GN   OrderedLocusNames=Halsa_1395 {ECO:0000313|EMBL:ADQ14822.1};
OS   Halanaerobium hydrogeniformans (Halanaerobium sp. (strain sapolanicus)).
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halanaerobium.
OX   NCBI_TaxID=656519 {ECO:0000313|EMBL:ADQ14822.1, ECO:0000313|Proteomes:UP000007434};
RN   [1] {ECO:0000313|EMBL:ADQ14822.1, ECO:0000313|Proteomes:UP000007434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=sapolanicus {ECO:0000313|Proteomes:UP000007434};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Begemann M.B., Mormile M.R., Wall J.D., Elias D.A., Woyke T.;
RT   "Complete sequence of Halanaerobium sp. sapolanicus.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADQ14822.1, ECO:0000313|Proteomes:UP000007434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=sapolanicus {ECO:0000313|Proteomes:UP000007434};
RX   PubMed=21602336; DOI=10.1128/JB.05209-11;
RA   Brown S.D., Begemann M.B., Mormile M.R., Wall J.D., Han C.S., Goodwin L.A.,
RA   Pitluck S., Land M.L., Hauser L.J., Elias D.A.;
RT   "Complete Genome Sequence of the Haloalkaliphilic, Hydrogen Producing
RT   Halanaerobium hydrogenoformans.";
RL   J. Bacteriol. 193:3682-3683(2011).
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; CP002304; ADQ14822.1; -; Genomic_DNA.
DR   RefSeq; WP_013405903.1; NC_014654.1.
DR   AlphaFoldDB; E4RL58; -.
DR   STRING; 656519.Halsa_1395; -.
DR   KEGG; has:Halsa_1395; -.
DR   eggNOG; COG0543; Bacteria.
DR   HOGENOM; CLU_003827_1_0_9; -.
DR   OMA; AGQFIIL; -.
DR   OrthoDB; 9778346at2; -.
DR   Proteomes; UP000007434; 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; 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   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:UP000007434}.
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   276 AA;  30456 MW;  C533042C9D7272D7 CRC64;
     MYEVLAKEKL APTIKKLTVK APLIAEKTQP GNFIILRVDE KGERIPLTVA DYDREKGSIT
     IIFQEVGYST KLLGKMEKGD QIRDIVGPLG HHIDMEGYDK VVLLGGGTGT ALLYPKVKGF
     YEMGAEVISI TGARTKKLII LEDDLRKFSD KLYIATDDGS YGHHGFVTEI LKDVLEEEED
     IDLVVAIGPV PMMKAVADMT KEYGIETIVS LNAIMVDGTG MCGACRITVG GETKFTCVDG
     PAFDAHKVDF AELMNRLNFY TNEEEKIKDN AVKEEI
//
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