ID A0A0B0ELG2_9BACT Unreviewed; 702 AA.
AC A0A0B0ELG2;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=FeS molybdopterin oxidoreductase protein {ECO:0000313|EMBL:KHE91545.1};
DE EC=1.7.99.4 {ECO:0000313|EMBL:KHE91545.1};
GN Name=napA {ECO:0000313|EMBL:KHE91545.1};
GN ORFNames=SCABRO_02755 {ECO:0000313|EMBL:KHE91545.1};
OS Candidatus Scalindua brodae.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Scalinduaceae; Scalindua.
OX NCBI_TaxID=237368 {ECO:0000313|EMBL:KHE91545.1, ECO:0000313|Proteomes:UP000030652};
RN [1] {ECO:0000313|EMBL:KHE91545.1, ECO:0000313|Proteomes:UP000030652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU1 {ECO:0000313|EMBL:KHE91545.1};
RA Speth D.R., Russ L., Kartal B., Op den Camp H.J., Dutilh B.E., Jetten M.S.;
RT "Draft genome of anammox bacterium scalindua brodae, obtained using
RT differential coverage binning of sequence data from two enrichment
RT reactors.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KHE91545.1}.
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DR EMBL; JRYO01000193; KHE91545.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B0ELG2; -.
DR PATRIC; fig|237368.3.peg.2982; -.
DR eggNOG; COG0243; Bacteria.
DR Proteomes; UP000030652; Unassembled WGS sequence.
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:0008940; F:nitrate reductase activity; IEA:UniProtKB-EC.
DR CDD; cd00508; MopB_CT_Fdh-Nap-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; 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 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.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KHE91545.1}.
FT DOMAIN 3..59
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 702 AA; 77602 MW; 734A43F9C9130077 CRC64;
MTVQWKKTTC SYCGLGCGLM VGLDDGKVVD IKGMKGHPVN DGMVCTLPAN YVPIFEAEGR
LSDPMIRRDG KLTQVNWDEA INHVAGGLKG IIDRHGPNSI ALYMGGTCLN EEYYIANKFM
KAAIGTNNIE CTTRLCTSSS AMGFISTIGA DAPPACYDDV EEADLIFIAG NNMAVSVPAI
FARVRAAKKK NGTKVIVVDP RKTETALIAD IHLQIQPGTD VALNNALAHV LFEEGYVDEE
SVGKVASGLS DLKKLVKRYA PLRVSQITGC PEDQIREAAR LIGRSKTMLV SWFQGYGHST
QSVFKNNTLH NLWLLTDNFC RPGAGPLSIT GESNALGNRW VGGLSHLLPG MRMVINSQHR
QELADYWGIP VEKMQSTPGR SIIEMIEGLH SGDVRALWII SANPAASLPD TKWVRDGLSK
AELLIVQDIF HPTESTMMAD VVFAGAHWIE KTGTFISSER RIELVDQIVE SYGNVKPDYD
IICRIANAMG FENDFQYASS EEVFEELKKI TKGRLCDMSG VTYERLRNKV GLQLPCPTED
HPGTERLFTD RQFPRPDGRA ALLPREYKKP CEIPDKEYPY ILITGRLQWH FNTRTRTGRV
SSLDSKARDN FVEINPVTAS QLDIVDGDEV EVTSRRGSVS GAVRIIDSML PNTIFMPMHF
GNTLNVGDGR LANLLTNHVC DLHSKQPEYK YSVVKISKAD QT
//
