ID K9QZ76_NOSS7 Unreviewed; 725 AA.
AC K9QZ76;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Anaerobic dehydrogenase, typically selenocysteine-containing {ECO:0000313|EMBL:AFY50097.1};
GN OrderedLocusNames=Nos7524_4338 {ECO:0000313|EMBL:AFY50097.1};
OS Nostoc sp. (strain ATCC 29411 / PCC 7524).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=28072 {ECO:0000313|EMBL:AFY50097.1, ECO:0000313|Proteomes:UP000010378};
RN [1] {ECO:0000313|Proteomes:UP000010378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29411 / PCC 7524 {ECO:0000313|Proteomes:UP000010378};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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; CP003552; AFY50097.1; -; Genomic_DNA.
DR RefSeq; WP_015140509.1; NC_019684.1.
DR AlphaFoldDB; K9QZ76; -.
DR SMR; K9QZ76; -.
DR STRING; 28072.Nos7524_4338; -.
DR KEGG; nop:Nos7524_4338; -.
DR PATRIC; fig|28072.8.peg.4745; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_4_3; -.
DR OrthoDB; 9805142at2; -.
DR Proteomes; UP000010378; 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 InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
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 PIRSF; PIRSF000144; CbbBc; 2.
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.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 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:UP000010378}.
FT DOMAIN 2..70
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 22..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 80430 MW; 4ABA9B7F2B5BDEA4 CRC64;
MPESTKTVCP YCGVGCGLEV SPPAQPNTAT NRDSQGNPVW RVRGDKSHPS SQGMVCVKGA
TIAESLDKNR LHYPMVRDSL DQEFRRVSWD EAFDIITQRI QTVRFTQGAE AICMYGSGQF
QTEDYYIAQK LMKGCLGTNN FDANSRLCMS SAVSGYIQSF GSDGPPCCYE DLELTDCAFL
IGTNTAECHP IVFNRLAKYH KKNRHVKMIV VDPRRTPTAE AADLHLAIRP GTDIDLLNGI
AHLLMRWQMI DVGFIDDCTS NFSAYAEVIR HYSPEVVARQ CGISVADLET AARYWGQAQR
VLSLWSMGVN QSTEGTAKVR TIINLHLMTG QIGKPGAGAF SLTGQPNAMG GREAGGLAHL
LPGYRSVKNP QHRAEVEAFW RLQPGQISPH PGLTAWEMIL GLEAGNVGLL WIAATNPAVS
MPDLERTKKA LLRSPFTIYQ DAYYPTETSA FAHVLLPAAQ WSEKIGVMTN SERRVTLSQA
FRQPPGEAKA DWEIFAEVGR RLSFGDKFAF NNSAQVYTEF VQLTKGRTCD MTGISHEQLR
QEGATQWPHP KEGTGAKRLY TDLRFPTSDG RAKFAAYYSK GLAEPPDPDY PFVLTTGRLY
GHWHTQTRTG RIEKIRSMHP EPFIEIHPRD AAKLEIIDSQ MIEVRSRRGT AQFKAKVTKA
IAPGTVFVPM HWGSLWADNA EANALTHPES CPDSFQPELK ACAVQLIPIS LKITAKTSQL
QSTQW
//
