ID F5T1Q5_9GAMM Unreviewed; 863 AA.
AC F5T1Q5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Anaerobic dehydrogenase, typically selenocysteine-containing protein {ECO:0000313|EMBL:EGL53048.1};
GN ORFNames=MAMP_00158 {ECO:0000313|EMBL:EGL53048.1};
OS Methylophaga aminisulfidivorans MP.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=1026882 {ECO:0000313|EMBL:EGL53048.1, ECO:0000313|Proteomes:UP000003544};
RN [1] {ECO:0000313|EMBL:EGL53048.1, ECO:0000313|Proteomes:UP000003544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP(T) {ECO:0000313|Proteomes:UP000003544};
RX PubMed=21685284; DOI=10.1128/JB.05403-11;
RA Han G.H., Kim W., Chun J., Kim S.W.;
RT "Draft genome sequence of Methylophaga aminisulfidivorans MP T.";
RL J. Bacteriol. 193:4265-4265(2011).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. NasA/NapA/NarB subfamily.
CC {ECO:0000256|ARBA:ARBA00008747}.
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:EGL53048.1}.
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DR EMBL; AFIG01000003; EGL53048.1; -; Genomic_DNA.
DR AlphaFoldDB; F5T1Q5; -.
DR STRING; 1026882.MAMP_00158; -.
DR eggNOG; COG0243; Bacteria.
DR Proteomes; UP000003544; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
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 GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR CDD; cd02791; MopB_CT_Nitrate-R-NapA-like; 1.
DR CDD; cd02754; MopB_Nitrate-R-NapA-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR041957; CT_Nitrate-R-NapA-like.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF04324; Fer2_BFD; 1.
DR Pfam; PF00384; Molybdopterin; 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000003544}.
FT DOMAIN 43..466
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 567..678
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
FT DOMAIN 813..862
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
SQ SEQUENCE 863 AA; 94936 MW; 4B9B343D7E157173 CRC64;
MLATPLQNGT VQIEGDETHP ANLGRLCSKG SALGETVDLG NRLLHPKVHG KRVSWDEAIM
SVARGFSDII AKHGPESVAF YVSGQVLTED YYTANKLMKG FIGGANIDTN SRLCMSSAVA
AYKRAFGSDT VPCSYEDIEL ADLVILAGSN LAWCHPVIFQ RLRQAKEDRP EMKIVVIDPR
KTSTCDIADL HLSVKPGTDA TLFNGLLHYL KKEDYLDLEF LEAHTEGFAA AMTAAKTSAG
SIPQVAAVTE LQEQDIVKFY QLFASTEKVV TVYSQGINQS TSGTDKCNSI INCHLATGRI
GKPGMGPFSF TGQPNAMGGR EVGGLSNQLA AHMEITNPEH HDRVSRFWKA DNLATENGAK
AIDMFNEVAS GKIKAIWIMA TNPVVSLPDA DKVKAALEKC ELVVVSECEK FTDTTELADI
LLPAAAWGEK DGMVTNSERR ISHQRAFLPL PGEARPDWWI ITQVARKMGF EAAFPFEKPA
DVFREHAQLS AFENDGERDF NIGGLADISD EDYDNLVPVQ WPVMANTEMG TARLFTDKRF
FTPSGKARMI SVEPKLPFNP TTEAYPLVLN TGRIRDQWHT MTRTGRAVRL NAHIPEPMVQ
IHPLDAATFE LVDGALAEVS SQWGEMIVRV VVTDEQRPGS IFVPIHWSSQ YASMARVDAL
VASVYDPVSG QPESKHTPVT IRAYQPVWHG FILSRHPITV KDANYWVKVR GAQFWRYEIA
GQQSLDDPAK WAQQHLGEEG EWLDFTDAKA GRYRAGQIKR NRLEGVVFIA PSHDLPARSW
LSQLFSLNSL SDAERYSLLV GQPSQGQKDA GQIVCSCFGV GQNTLNEAIQ SGHVNSVDEI
GQKLKAGTNC GSCVPELKKL LAH
//