PYRKH_THEMA
ID PYRKH_THEMA Reviewed; 282 AA.
AC Q9X1X4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit homolog;
DE AltName: Full=Dihydroorotate oxidase B, electron transfer subunit homolog;
GN OrderedLocusNames=TM_1639;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the PyrK family. {ECO:0000305}.
CC -!- CAUTION: Lacks the first cysteine that binds the 2Fe-2S complex.
CC {ECO:0000305}.
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DR EMBL; AE000512; AAD36706.1; -; Genomic_DNA.
DR PIR; G72230; G72230.
DR RefSeq; NP_229439.1; NC_000853.1.
DR PDB; 4YLF; X-ray; 2.30 A; A/C=1-276.
DR PDB; 4YRY; X-ray; 2.40 A; A/C=1-276.
DR PDBsum; 4YLF; -.
DR PDBsum; 4YRY; -.
DR AlphaFoldDB; Q9X1X4; -.
DR SMR; Q9X1X4; -.
DR STRING; 243274.THEMA_06050; -.
DR EnsemblBacteria; AAD36706; AAD36706; TM_1639.
DR KEGG; tma:TM1639; -.
DR PATRIC; fig|243274.5.peg.1658; -.
DR eggNOG; COG0543; Bacteria.
DR InParanoid; Q9X1X4; -.
DR OMA; AGQFIIL; -.
DR BRENDA; 1.6.1.4; 6331.
DR Proteomes; UP000008183; 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 Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
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 Pfam; PF10418; DHODB_Fe-S_bind; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF006816; Cyc3_hyd_g; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Electron transport; FAD; Flavoprotein; Iron;
KW Iron-sulfur; Metal-binding; Reference proteome; Transport.
FT CHAIN 1..282
FT /note="Dihydroorotate dehydrogenase B (NAD(+)), electron
FT transfer subunit homolog"
FT /id="PRO_0000148372"
FT DOMAIN 2..100
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 225
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT STRAND 6..14
FT /evidence="ECO:0007829|PDB:4YLF"
FT STRAND 16..25
FT /evidence="ECO:0007829|PDB:4YLF"
FT HELIX 27..32
FT /evidence="ECO:0007829|PDB:4YLF"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:4YLF"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:4YLF"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:4YLF"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:4YLF"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:4YLF"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:4YLF"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:4YLF"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:4YLF"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:4YLF"
FT HELIX 119..126
FT /evidence="ECO:0007829|PDB:4YLF"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:4YLF"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:4YLF"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:4YLF"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:4YLF"
FT STRAND 155..169
FT /evidence="ECO:0007829|PDB:4YLF"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:4YLF"
FT TURN 175..181
FT /evidence="ECO:0007829|PDB:4YLF"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:4YLF"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:4YLF"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:4YLF"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:4YLF"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:4YLF"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:4YLF"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:4YLF"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:4YLF"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:4YLF"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:4YLF"
FT HELIX 253..260
FT /evidence="ECO:0007829|PDB:4YLF"
FT HELIX 267..273
FT /evidence="ECO:0007829|PDB:4YLF"
SQ SEQUENCE 282 AA; 31091 MW; BEA9816C469D2AF1 CRC64;
MGGTALNEIV KKVKIAEDVF DFWIHSPSVS KEARPGQFVV IRLHEKGERI PLTVADTKPE
EGLFRMVVKV VGKTTHELSL KKEGDTILDV VGPLGNPSEI ENYGNVLLVG GGVGIATLYP
IAKALKEAGN NITTVLGART KDYLIMVDEF KEISDVLLVT DDGSAGMKGV VTDAMDKLFR
ERKFDICWAV GPTIMMKFCT LKAREFGVPI WVSLNPIMVD GTGMCGACRV TVSGQIKFAC
VDGPEFRGEE VDWDELLKRL AQYREQEKIS YERFLKTAGE SE