ID S6HHI4_9GAMM Unreviewed; 776 AA.
AC S6HHI4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Oxidoreductase alpha (Molybdopterin) subunit {ECO:0000313|EMBL:EPJ48274.1};
GN ORFNames=OFPII_06860 {ECO:0000313|EMBL:EPJ48274.1};
OS Osedax symbiont Rs1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae.
OX NCBI_TaxID=1330036 {ECO:0000313|EMBL:EPJ48274.1, ECO:0000313|Proteomes:UP000014822};
RN [1] {ECO:0000313|EMBL:EPJ48274.1, ECO:0000313|Proteomes:UP000014822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rs1 {ECO:0000313|Proteomes:UP000014822};
RA Yi H., Goffredi S.;
RT "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT Osedax worms: functional variation and environmental selection.";
RL Submitted (MAY-2013) 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:EPJ48274.1}.
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DR EMBL; ASZJ01000039; EPJ48274.1; -; Genomic_DNA.
DR AlphaFoldDB; S6HHI4; -.
DR PATRIC; fig|1330036.3.peg.644; -.
DR Proteomes; UP000014822; 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:UP000014822}.
FT DOMAIN 108..491
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 652..709
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 776 AA; 85133 MW; A032D99772A0AD59 CRC64;
MTKKKTSNYK GSAGGWGALA STTKHLLKSR RPIKNIVSLL KTNQDQGFDC PGCAWGDTKG
HSISFCENGA KAVNWEATAK RVGADFFAKY SVSYLEKQSD YYLEYQGRLT QPMRYNSDTD
HYEPITWDDA FALIATHLNN LESPNQAEFY TSGRASNEAA FMYQMMVRSF GTNNFPDCSN
MCHEASGVAM KETIGVGKGT VSLDDFDLAD AIFVFGQNPG TNHPRMLESL RQASRRGATV
VSINNLRERG LERFTNPQSP IEMLTNGHTT ISKHYYTPKL GGDMALIRGV VKALLTLDKA
AIDRGEPSLL AVDFLAEHTS GLDDYLHLVR ATAWEALIEQ SGVSRADMEH IATVYANSEK
VICSWAMGLT QHKHSVITLQ EIINLLLLRG NIGKPGAGAC PVRGHSNVQG DRTMGINEKA
PAALLDNLEQ LLGQKMPREA GHNAIQAVQA MTAGQSKVFI ALGGNFAAAM PDTHVTRRAM
AKCDLVVNIS TKLNRSHLTP GKDALILPCL GRTELDITEN GQQRITVEDS MSMVHSSGGV
LPPASKQLKS EVEIVARIAN ATLKDSSIDW LALAADNCKI RDLIEQCIDG FANFNQRLAA
PGGFYLGNPA AQRVWLTDTA LANIKSNPLP EHLIAEQITS QRRKKKQSGK IFTLQTMRSH
DQYNTTIYGF NDRYRGVKGQ RNVIFMNVDD MQHLGLSAEQ EVTITSHWHD DSERSVSGFK
VIAYDIPTGN MAAYYPETNP LIALESYGDQ SFTPTSKAIA ISISTAKSSS IIKRGE
//
