ID   A0A1G7WZ44_9RHOO        Unreviewed;       947 AA.
AC   A0A1G7WZ44;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Sulfide dehydrogenase (Flavoprotein) subunit SudA /sulfide dehydrogenase (Flavoprotein) subunit SudB {ECO:0000313|EMBL:SDG76600.1};
GN   ORFNames=SAMN05660652_00665 {ECO:0000313|EMBL:SDG76600.1};
OS   Propionivibrio dicarboxylicus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Propionivibrio.
OX   NCBI_TaxID=83767 {ECO:0000313|EMBL:SDG76600.1, ECO:0000313|Proteomes:UP000198607};
RN   [1] {ECO:0000313|EMBL:SDG76600.1, ECO:0000313|Proteomes:UP000198607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5885 {ECO:0000313|EMBL:SDG76600.1,
RC   ECO:0000313|Proteomes:UP000198607};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNCY01000001; SDG76600.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7WZ44; -.
DR   STRING; 83767.SAMN05660652_00665; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000198607; Unassembled WGS sequence.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd06219; DHOD_e_trans_like1; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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; IPR019480; Dihydroorotate_DH_Fe-S-bd.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR42783; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   PANTHER; PTHR42783:SF3; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   Pfam; PF10418; DHODB_Fe-S_bind; 1.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 2.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000198607}.
FT   DOMAIN          211..282
FT                   /note="Dihydroprymidine dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF14691"
FT   DOMAIN          310..616
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          881..921
FT                   /note="Dihydroorotate dehydrogenase electron transfer
FT                   subunit iron-sulphur cluster binding"
FT                   /evidence="ECO:0000259|Pfam:PF10418"
FT   REGION          565..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        570..586
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   947 AA;  103605 MW;  6F6888E5834CD0A3 CRC64;
     MSQATPNPQD DLYRYLNASE SLESTRSQIE ALEQSDAVNA FHNQMELLKR RLLQEPQAFR
     EMFIADGANA IVWEFQQPEL SESFINTFWE FLLRDDDISK VLMRFVWNVP LGLKRKFVKA
     LDQHLSDRYP MFKGLSNGWP ADSFIPPYIR SPEERSTDFE LVNQGYLGYM NTGLTAREVD
     MLVWLEVLRD KQCEERPCEI GLHVAGKADP KGGCPVKIHI PQVLNLMGNG RFREAMELIE
     SCNPLPNVTG RVCPQELQCQ GVCAHTKQPI EIGQLEWFLP QREKVVNPDG VAERFAGVPN
     PWEQAVKPPI AIVGSGPAGL INAYLLAAEG YPVTVFEAFH ALGGVLRYGI PEFRLPNSLI
     DDVVAKIKLL GGKFVQNFVV GKTATLQDLK NAGFWRIFVG SGAGLPRFMN IPGEHLLNVM
     SANEFLTRVN LMQGLREDYE TPLPETRGKE VLIIGGGNTA MDAARTARRL GGNVTIVYRR
     TRSEMPARVE ELHHALEEGI QLKVLRSPCE FIGDDKTHFV MATTLEVIAL GEPDASGRRS
     PAPTGEKETV KADLVIMALG NDPNPIIRDS EPSLKTTRGG SIELGTKGSM QTSLNGIYSG
     GDAARGGSTA IRAAGDGQAA AREIVGEINM SAAEIAGMVE QAKAYTELGA TPQTIVDKID
     LAGGIVEFIV KAPMIAKSAR AGQFVRVLAW PDGELIPLTL ADWDEKEGTI CLVVQGMGTT
     SLGINKMKIG ESFAGIAGPL GLPSELHHYD PKKQTVVFTA GGVGLPPVYP IAREHLRLGN
     HVTLISGFRS SSLLFWIAEN ERVGKLKAEF GDLLDVIYCS NDGSFGIHGF VTTPLEEMLK
     NGKKSKGRDI AEVVTIGPPL MMRAVSDLTK PYGVKTVASL NSIMVDATGM CGACMVPVNL
     DGRMVRKHAC VDGPEIDSHI IDWDKFLPRF GLFKPQEQAS KVKHGFA
//