ID A0A0K2GE66_NITMO Unreviewed; 958 AA.
AC A0A0K2GE66;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:ALA59246.1};
GN ORFNames=NITMOv2_2838 {ECO:0000313|EMBL:ALA59246.1};
OS Nitrospira moscoviensis.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=42253 {ECO:0000313|EMBL:ALA59246.1, ECO:0000313|Proteomes:UP000069205};
RN [1] {ECO:0000313|EMBL:ALA59246.1, ECO:0000313|Proteomes:UP000069205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSP M-1 {ECO:0000313|EMBL:ALA59246.1,
RC ECO:0000313|Proteomes:UP000069205};
RX PubMed=26305944; DOI=10.1073/pnas.1506533112;
RA Koch H., Lucker S., Albertsen M., Kitzinger K., Herbold C., Spieck E.,
RA Nielsen P.H., Wagner M., Daims H.;
RT "Expanded metabolic versatility of ubiquitous nitrite-oxidizing bacteria
RT from the genus Nitrospira.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:11371-11376(2015).
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 -!- 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}.
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DR EMBL; CP011801; ALA59246.1; -; Genomic_DNA.
DR RefSeq; WP_053380301.1; NZ_CP011801.1.
DR AlphaFoldDB; A0A0K2GE66; -.
DR STRING; 42253.NITMOv2_2838; -.
DR KEGG; nmv:NITMOv2_2838; -.
DR PATRIC; fig|42253.5.peg.2805; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000069205; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 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:UniProtKB-KW.
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; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041957; CT_Nitrate-R-NapA-like.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 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 Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000069205}.
FT DOMAIN 35..91
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 958 AA; 107275 MW; B85ECF3486DB6C1C CRC64;
MKETRDSIAD VWGPRTPYRD QWPVRVDERT VAQPDRWVPS ACLLCSYGCG IDIGVKDGRI
VGVRGRESDR TNHGRLGPKG LHGWAANHSA DRLTTPLIRR KGELQPASWD EAMDLIVRRS
KELIDRHTGN SIAFYTSGQL YLEEYYTLGI IGKAGIGTPH MDGNTRLCTA TADFSLKESF
GTDGQPGSYE DVDLADALML VGHNVASQQT VMWMRILDRR AGPNPPKLVV IDPRRTDTAK
EADVHLALRL GTNVALLNGL QHLLIKHGWI DRSFIETHTV GFEKLAHLVS TWTSDRVERV
TGVPQRELMK AAEIIGRTPR LMSTVLQGVY QSMQATAAAV QINNIQLLRG MIGKPGCTVL
QMNGQPTAEN TRECGADGDF PAFRNWENED HMQEMARIWN VERAKLPTYA PPTHAMQIFR
YAEEGTVKML WISGTNPAVS LPELARIRRI LNLRSLFVVV QDAFRTETTE HADVVLPAAL
WGEKTGCYTN VDRTVHLSEK AIEPPGQATS DFDIFVDYAR RMNFSDKDGA PLVKWATPED
CFEAWKLCSK GRPCDYSGMS YAKLRGSAGI QWPCTEQAPN GTPRLYNDHR FNTQADYCET
YGHDLTTGAV NTPEKYRARD PQGKAFLHAV EYQPPHEEPD EDYPFRVTTG RIVYHWHTRT
KTGRSRELNE AAPDAFIQMH EDDAARLGVR DGDWVEVASR RGHVTARAKL GDILPGHLFI
PFHYGYWDDP DRARAANELT LTEWDPVSKQ PYFKFSAARA KKVSGAPIVE KVAQVAESVT
GKLKNTATEL MDMPGKIAKA VSTADDERPV NVFLGMAFQG ERHLVEAFKQ VAQQHMAEPD
IHATCRLMAS WSQEQAEGLK PFIAAYHKDR SKDPEGSVKS LFEGPRSGGL GLLRDLHDLW
LAANEVHLDY EAVKQAAKAL HDQALVETCE RHLNQTDRQL AWLRTRIDQA SPQTLVVS
//
