ID G5ZY28_9PROT Unreviewed; 771 AA.
AC G5ZY28;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Anaerobic dehydrogenase, typically selenocysteine-containing {ECO:0000313|EMBL:EHI49014.1};
GN ORFNames=HIMB100_00009300 {ECO:0000313|EMBL:EHI49014.1};
OS SAR116 cluster alpha proteobacterium HIMB100.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; SAR116 cluster.
OX NCBI_TaxID=909943 {ECO:0000313|EMBL:EHI49014.1, ECO:0000313|Proteomes:UP000004261};
RN [1] {ECO:0000313|EMBL:EHI49014.1, ECO:0000313|Proteomes:UP000004261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain HIMB100 {ECO:0000313|Proteomes:UP000004261};
RX PubMed=22675578; DOI=10.4056/sigs.1854551;
RA Grote J., Bayindirli C., Bergauer K., Carpintero de Moraes P., Chen H.,
RA D'Ambrosio L., Edwards B., Fernandez-Gomez B., Hamisi M., Logares R.,
RA Nguyen D., Rii Y.M., Saeck E., Schutte C., Widner B., Church M.J.,
RA Steward G.F., Karl D.M., Delong E.F., Eppley J.M., Schuster S.C.,
RA Kyrpides N.C., Rappe M.S.;
RT "Draft genome sequence of strain HIMB100, a cultured representative of the
RT SAR116 clade of marine Alphaproteobacteria.";
RL Stand. Genomic Sci. 5:269-278(2011).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
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:EHI49014.1}.
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DR EMBL; AFXB01000007; EHI49014.1; -; Genomic_DNA.
DR AlphaFoldDB; G5ZY28; -.
DR STRING; 909943.HIMB100_00009300; -.
DR PATRIC; fig|909943.3.peg.943; -.
DR eggNOG; COG0243; Bacteria.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000004261; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02793; MopB_CT_DMSOR-BSOR-TMAOR; 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 Gene3D; 3.90.55.10; Dimethylsulfoxide Reductase, domain 3; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041954; CT_DMSOR/BSOR/TMAOR.
DR InterPro; IPR041460; Molybdopterin_N.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR PANTHER; PTHR43742:SF10; TRIMETHYLAMINE-N-OXIDE REDUCTASE 2; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF18364; Molybdopterin_N; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000004261}.
FT DOMAIN 9..49
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 53..510
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 625..744
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
FT REGION 714..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 771 AA; 85503 MW; AF2FAAC12B6570AD CRC64;
MKTTRTSLTS NHWGVGLVET IDDEIIGVHP FAEDPEPSDL NKNIVESIHG EARVLRPAFR
KSWLENGPGR SSVERGKDTF VEVEWDEALE RIANELSRVR NTFGNESIFA GSYGWASAGR
FHHAQSQLKR FLNTQGGFVG SEGNYSYNAA LVFMPHVVGD FRESVAAATR WNVIKNHTKR
VVCFGGVPTR NGQISDGGIF KHRLPGNLKD CADSGVKFIN ISPLQSDLLP ELEAEWMPTW
PGSDTAIMMG LAYTLLSENL HNQEFLDTYT VGFPQIAAYI MGKTDGHPKT AEWAEKQSGV
KADRIKSLAR EMVQNRTMIS VAAGVQRGDY GEQPLWMAVT LAAMLGQIGL PGGGYTIAYA
VNGNVGNTER LFRAGALSQG TNPVKSYIPV AMIADLLLNP GGHYQYNGRN CTFNDIRLVW
WAGGNPFHHH QDLNRLRKAF QRPETIIVNE INWTSTARHA DIILPVASPQ ERTDFGAGKS
DNALIPMPAA ISPVGSSRTE YEIYAELAER LGNRELFTEN KTSNDWLNEL WEVTRERGRQ
AGMNLPNWKD FISGDAIELP DPSPNQVFLS EFRTDPHAHP LKTPSGKIEL YSEVIASFAL
EDCPGHATWF PPRDVKVGLK KEYPLYLLSG QPATRLHSQF DNGTYSRSQK IDGREPVFIH
PDDAALRGIQ TGDIVELFNK RGACLAGARV TNEIARGNVF LWTGAWYDPD FNVNQDRDRH
GNPNTLTHDE KTSSLSQSPA AHSALVDIQK FAGPVPDITV HHQPEFTILA E
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