ID A0A1A8XWY6_9PROT Unreviewed; 911 AA.
AC A0A1A8XWY6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:SBT09142.1};
GN ORFNames=ACCAA_670064 {ECO:0000313|EMBL:SBT09142.1};
OS Candidatus Accumulibacter aalborgensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=1860102 {ECO:0000313|EMBL:SBT09142.1, ECO:0000313|Proteomes:UP000199169};
RN [1] {ECO:0000313|EMBL:SBT09142.1, ECO:0000313|Proteomes:UP000199169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3 {ECO:0000313|EMBL:SBT09142.1};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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}.
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DR EMBL; FLQX01000146; SBT09142.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A8XWY6; -.
DR STRING; 1860102.ACCAA_670064; -.
DR Proteomes; UP000199169; Unassembled WGS sequence.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
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:0045333; P:cellular respiration; IEA:UniProt.
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; 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; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
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; 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.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 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:UP000199169}.
FT DOMAIN 2..58
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 911 AA; 97543 MW; DF5A3DA6D77B16E8 CRC64;
MNKPVKSTCC YCGVGCGLLV DTEAGQIVGV RGDPDHPANA GRLCTKGASL HLTARPDDRL
LYPELRRRRG LPRQRVGWDD ALDHAAERFA AIIRSHGPDS VAFYVSGQLL TEDYYVFNKL
AKGLIGTNNI DTNSRLCMSS AVAGYKQTLG ADAPPCCYED IALTDCLLIA GANPAVAHPI
VFRRIEDARA ANPALRIIVI DPRRSESAAI ADLHLALKPG TDIALYNGLL NVMLAEELVD
RPYIAAHTEG FAALEQIVAA YPPAVVAEIC GLAEADIITA ARWFGTAGAA LSLYCQGLNQ
SAHGTHNNAA LIHLHLASAQ IGRPGAGPFS LTGQPNAMGG REVGGLANVL SAHRDLANAE
HRAEVARLWG VPSVPEQPGK TAVELFAALK SGEIKAVWIA CTNPAQSLPD QTAVRAALQV
ADFVVLQEAY AHTDTAAWAD LMLPATTWGE KEGTLTNSER RITHIMPAVA GPGEARHDWQ
IVVDFARRLG ARLEQPLAEE LFPYTGSEAI FNEHRESTRG RDLDITGISY ALLDARGPQQ
WPLPEGATSG RQRLYADGIF PTASGRARFV GVEHRPSAET TDAAHPISLL SGRLRDQWHG
MSRTGTVARL FNLDDEPLLS MHPADLSQRG LTTGDLATVD SRRGSIVIRV RGDGGLKPGR
AWLPMHWGSQ FMNSAGVNAL TLSATDPYSF QPELKHAAVA VAKAALPWQL VVLRKTGAGE
STAHALLARA RTLLGEFAFA SVGLYGRAEP LVVFRAANAH ALPESRLREI DTLFGLGDDD
AAIVYADHRR QISKRAVAPD GRLIGVRLAG ETQAQSWLKE VMADETLDAA LIRWAVAPIG
TRPGRLPQCS RVLCNCADIT VAQITADLAT GATLAMVQDK RKCGTFCGSC LPELKQMIAS
QALGTVSETI V
//
