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Database: UniProt
Entry: A0A2P5SWT4_9GAMM
LinkDB: A0A2P5SWT4_9GAMM
Original site: A0A2P5SWT4_9GAMM 
ID   A0A2P5SWT4_9GAMM        Unreviewed;       754 AA.
AC   A0A2P5SWT4;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=CbbBc protein {ECO:0000313|EMBL:PPI86789.1};
GN   ORFNames=CRV10_00845 {ECO:0000313|EMBL:PPI86789.1};
OS   Candidatus Pantoea edessiphila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=2044610 {ECO:0000313|EMBL:PPI86789.1, ECO:0000313|Proteomes:UP000296144};
RN   [1] {ECO:0000313|EMBL:PPI86789.1, ECO:0000313|Proteomes:UP000296144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SoEL {ECO:0000313|EMBL:PPI86789.1,
RC   ECO:0000313|Proteomes:UP000296144};
RX   PubMed=29420776;
RA   Otero-Bravo A., Goffredi S., Sabree Z.L.;
RT   "Cladogenesis and Genomic Streamlining in Extracellular Endosymbionts of
RT   Tropical Stink Bugs.";
RL   Genome Biol. Evol. 10:680-693(2018).
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PPI86789.1}.
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DR   EMBL; PDKU01000001; PPI86789.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P5SWT4; -.
DR   OrthoDB; 5287431at2; -.
DR   Proteomes; UP000296144; Unassembled WGS sequence.
DR   GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR   CDD; cd02787; MopB_CT_ydeP; 1.
DR   CDD; cd02767; MopB_ydeP; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR037951; MopB_CT_YdeP.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR010046; Mopterin_OxRdtse_a_bac.
DR   InterPro; IPR041953; YdeP_MopB.
DR   NCBIfam; TIGR01701; Fdhalpha-like; 1.
DR   PANTHER; PTHR43105:SF4; PROTEIN YDEP; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   PIRSF; PIRSF000144; CbbBc; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000296144}.
FT   DOMAIN          109..484
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          639..746
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   754 AA;  84997 MW;  40C876F204145CF9 CRC64;
     MKFKNKIKPY NSAAGGWDSI KSTARFIFDS KATFKSIRNL LKINKQDGFD CPGCAWGNDN
     KSIFDFCENG AKAVAWETTN RSVDKNFFAR NSVNYLYKQN DHFLEYQGRL VDPVYYNSRN
     NHYEFISWDN AFELIAKHIN TMDHPNQLEL YTSGRTSNEG AWLYQLFGRL IGTNNFPDCS
     NMCHEASGIG LNLSIGTVKG TVRLDDFNHA DAIFVFGQNP GTNHPRMLHS LRRASDRGAK
     IVVFNTLRER GLERFADPKR PIEVITVVES IINTAYYQPN LGGDMAAVRG IVKCLLEENR
     QTNDVFNCNF IKDKTKGINE YLKVVDSTKW NEITIQSGLT KKQIYEAALI YKNAKRVICT
     WGMGITQHKH SVNTVREIVN LQLLFGQIGK KGSGLCPVRG HSNVQGNRTM GINEKPDLAF
     LNKLEKYFDF KAPRSKGHNT IEALNAMLNG NVRVLISLGG NLAAAAPDYL RTKKALSSCG
     ITVHISTKLN RSHLIPGRES LILPTIGRTE IDKTNNRNQF ITVEDTFSMV HGSQGRCEPL
     SSQQRSEIAI ISEIAYKTLG DNKINWKALS SNYNLIRKQI ADIIPGFANL TKKCSVFKGF
     YLANAASQYV FNTASKKAQF SNALLPKSIF LNLNNDVNFT LQTLRSHDQY NTTIYGFDDR
     YRGVYGQRNV LFININDMNK LGFKTGQNVD IETVWNDAIK RSVKNFKLVP YNITSGNLAA
     YYPETNVLIP MDSFGDYSYT PTSKSVQVKL KLST
//
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