ID A0A0K2GIJ5_NITMO Unreviewed; 1145 AA.
AC A0A0K2GIJ5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Putative Nitrite oxidoreductase, alpha subunit {ECO:0000313|EMBL:ALA60417.1};
DE EC=1.7.99.4 {ECO:0000313|EMBL:ALA60417.1};
GN ORFNames=NITMOv2_4033 {ECO:0000313|EMBL:ALA60417.1};
OS Nitrospira moscoviensis.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=42253 {ECO:0000313|EMBL:ALA60417.1, ECO:0000313|Proteomes:UP000069205};
RN [1] {ECO:0000313|EMBL:ALA60417.1, ECO:0000313|Proteomes:UP000069205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSP M-1 {ECO:0000313|EMBL:ALA60417.1,
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).
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DR EMBL; CP011801; ALA60417.1; -; Genomic_DNA.
DR RefSeq; WP_053381280.1; NZ_CP011801.1.
DR AlphaFoldDB; A0A0K2GIJ5; -.
DR STRING; 42253.NITMOv2_4033; -.
DR KEGG; nmv:NITMOv2_4033; -.
DR PATRIC; fig|42253.5.peg.3980; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000069205; Chromosome.
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:0008940; F:nitrate reductase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.12440; -; 3.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF00384; Molybdopterin; 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.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:ALA60417.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000069205}.
FT DOMAIN 61..129
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1145 AA; 131925 MW; 1A79CBEEFB94001D CRC64;
MFLSRRQFLK VSAGTVAAVA VADKVLALTA LQPVIEVGNP LGDYPDRSWE RVYHDQYRYD
SSFTWCCSPN DTHACRIRAF VRNGVVMRVE QNYDHQTYED LYGNRGTFAH NPRMCLKGYT
FHRRVYGPYR LKGPLMRKGW KQWMDDGSPE LTPETKRKYK FDSRFLDDML RVSWDTAFTY
AAKAMIIVAT RYSGEAGARR LREQGYAPEM IEMMKGAGTR CFKHRAGMPV LGIVGKMGNT
RMNGGINALL DTWIRKVQPE QAQGGRYWSN YTWHGDQNPA HPWWSGAQGS DIDLSDMRFS
KLNTSWGKNF VENKMPEAHW KLECIERGAR VVVITPEYNP TAYRADYWMP LRPESDGSLF
LGAMKIIVDE NMHDIDFLKE FTDAPILVRT DTLQYLDPRD VIADYKLPDF SKSYSGRIQS
LKPEQIERLG GMMVWDLNKK QAVPLHREQV GWHYKNSGID AALNGTFRVK LLNGREIDAM
PVWQMYLVHF QDYDLDTVHQ ICRTPKDLIV RWARDSGTIK PAAIHNGEGT CHYFHQTINA
RGAAMVLIIC GNVGKFGTGQ HTWAGNYKAG TWTATPWSGA GIAVHTGEDP FNITTDPNVH
GKEIKTKSYY YGEEVGYWNH GDTALIVNTP KYGRKVFTGK THMPTPSKLR WVTNVNVLNN
SKHHYDMVRN VDPNIETLIT QDIEMTSDVN HNDIAFACNT WMEFTYPEMT VTVSNPWVQV
WKGGIRPLYD TRNDLDTFAG TAAKLSEMTG DKRMKDYFAM VYLNRVDVYV QRMLDASSTF
YGYSADTMLK SEKGWMVMVR TYPRHPFWEE TNESKPMWTR SGRYENYRIE PEAIEYGENF
ISHREGPEAT PYLPNAIFTT NPYCRPDDYG IPVTAQHHDD KTVRNIKLSW HEIKRHSNPL
WEKGYQFYCV TPKTRHRVHS QWSVNDWVQI YESNFGDPYR MDKRTPGVGE HQLHINPQAA
KDRGINDGDY VYVDGNPVDR PYRGWKPSDP YYKVARLMIR AKYNPSYPYH VTMAKHAPYV
STAKSVKGHE TRPDGRAIAV DTGYQSNFRY GAQQSFTRSW LMPMHQTDSL PGKHAIAWKF
KWGYQVDHHA INTTPKECLI RITKAEDGGI GARGPWEPVR TGFTPGQENE FMIKWLKGEH
IKIKV
//
