ID A0A0M2KBE9_9GAMM Unreviewed; 769 AA.
AC A0A0M2KBE9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=CbbBc protein {ECO:0000313|EMBL:KKF34602.1};
GN ORFNames=SY86_02680 {ECO:0000313|EMBL:KKF34602.1};
OS Erwinia tracheiphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=65700 {ECO:0000313|EMBL:KKF34602.1, ECO:0000313|Proteomes:UP000033924};
RN [1] {ECO:0000313|EMBL:KKF34602.1, ECO:0000313|Proteomes:UP000033924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BuffGH {ECO:0000313|EMBL:KKF34602.1,
RC ECO:0000313|Proteomes:UP000033924};
RA Shapiro L.R.;
RT "Erwinia tracheiphila.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KKF34602.1}.
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DR EMBL; JXNU01000003; KKF34602.1; -; Genomic_DNA.
DR RefSeq; WP_016192631.1; NZ_JXNU01000003.1.
DR AlphaFoldDB; A0A0M2KBE9; -.
DR STRING; 65700.SY86_02680; -.
DR PATRIC; fig|65700.7.peg.673; -.
DR Proteomes; UP000033924; 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; 2.40.40.20; -; 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:UP000033924}.
FT DOMAIN 109..489
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 646..752
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 769 AA; 84983 MW; 90C14D9532163F2C CRC64;
MKFKMKIKPY EASAGGWGSL EATTRFVFDS KQVIKNMRNL MRMNKARGFD CPGCAWGDDN
KSTLSFCENG AKAVTWEATR RYVDAAFFAK HSVTTLYQQS DYFLEYQGRL TEPLRYNRET
DHYEPISWDD AFRLIARHIH AMASPDQMEL YTSGRASNEA SWLYQLFGRM NGSNNFPDCS
NMCHEASGTG LKRSIGVGKG TVRLDDFDHA DAIFVFGQNP GTNHPRMLHS LRHAADHGAK
IVTFNTLRER GLERFADPQK LLEVVTSKAG TISSSYYQPN LGGDMAAIRG MVKALMEAHR
ASLEKGENGI FDTDFIEMHT EGMDAYLNVV DATSWQNITQ QSGLSEIQIR EAAAIYQHAD
RVICTWAMGI TQHKHSVATV REIVNLQLLF GQLGKKGAGL CPVRGHSNVQ GNRTMGIYEK
PSAEFLDSLA RHFDFEPPRK AGHNTVEALE AMLRHEVKVL IALGGNLAAA PDSPRTEEAL
RRCALTVHIS TKLNRSHLCP GAVDALILPT LGRSEQDCQS GGPQFITVED SFSMVHASEG
IGKPIADTQR SETAIVAGIG NAVLGSQKVD WLALTGDYNK IRDHIAATIP GFSNFNARCD
IKGGFYLGNA AAELCFNTRN NKAQFSDACL PTSLFPQLDN DVSVPFTLQT LRSHDQYNTT
IYGLDDRYRG IYGQREVLFI NADDMAMLGL EADDKVDIET LWNDGIVRKV SAFKLVPYNI
PRGNLAAYYP ETNPLVPLSS YGDDSGTPTS KSIPVKIVLS AVKASQRIA
//
