ID B2VKP5_ERWT9 Unreviewed; 768 AA.
AC B2VKP5;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:CAO96675.1};
GN OrderedLocusNames=ETA_16290 {ECO:0000313|EMBL:CAO96675.1};
OS Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS 4357 / Et1/99).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=465817 {ECO:0000313|EMBL:CAO96675.1, ECO:0000313|Proteomes:UP000001726};
RN [1] {ECO:0000313|EMBL:CAO96675.1, ECO:0000313|Proteomes:UP000001726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99
RC {ECO:0000313|Proteomes:UP000001726};
RX PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA Geider K.;
RT "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT bacterium in the genus Erwinia.";
RL Environ. Microbiol. 10:2211-2222(2008).
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}.
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DR EMBL; CU468135; CAO96675.1; -; Genomic_DNA.
DR RefSeq; WP_012441368.1; NC_010694.1.
DR AlphaFoldDB; B2VKP5; -.
DR STRING; 465817.ETA_16290; -.
DR KEGG; eta:ETA_16290; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_16_1_6; -.
DR OrthoDB; 5287431at2; -.
DR Proteomes; UP000001726; Chromosome.
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:UP000001726}.
FT DOMAIN 109..490
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 645..752
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 768 AA; 84311 MW; 67F3827D8309EF72 CRC64;
MKFKQAIKPY QAAAGGWGSL EATTRFVFDS KEVLKNMRNL MRMNKAKGFD CPGCAWGDDN
KSTFSFCENG AKAVTWEATR RHIGAEFFAQ YSVSALYQQS DYFLEYQGRL TEPLRYNRAT
DRYEPIGWQE AFELIASHIK AMDNPDQMEL YTSGRASNEA SWLYQLFGRM NGSNNFPDCS
NMCHEASGTG LKRSIGVGKG TIRLDDFDHA NAIFVFGQNP GTNHPRMLHS LRHAADHGAK
IVTFNTLRER GLERFADPQK PLEVVTSKSG TISSSYYQPN LGGDMAAVRG MVKVLAENHH
ARIAAGEKGL FDEAFIQANT EGVDAYLAMV DATGWPQIVK QSGLSEEQIR EAAAIYQSAD
RVICTWAMGI TQHKHSVDTV REIVNLQLLF GQLGKKGAGL CPVRGHSNVQ GNRTMGIDEK
PSKAFLDSLG EHFSFTPPRE IGHNTVQALE AMLRDEIKVL IALGGNLAAA APDSPRTEEA
LKRCGLTVQI STKLNRSHLC PGNQDALILP TLGRTEQDIQ ASGPQFITVE DSFSMVHASE
GVGKPIATTQ RSETWIVAGI AHAVLGSEKV DWLGLADDYN KIRDHIAATI PGFSDFNTRC
DIKGGFYLGN AAADLRFNTL NEKAQFSAPA LPATLFPQLD VDVPFTLQTL RSHDQYNTTI
YGLDDRYRGV YGQREVLFIN PEDLAELGYA AGDDVDIETL WNDGITRKVS GFKLVPYAIP
RGNLAAYYPE TNPLVPLSSF GDGSGTPTSK SIPVKITLSP VVDGLRIA
//
