ID D2R303_PIRSD Unreviewed; 764 AA.
AC D2R303;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:ADB18736.1};
GN OrderedLocusNames=Psta_4086 {ECO:0000313|EMBL:ADB18736.1};
OS Pirellula staleyi (strain ATCC 27377 / DSM 6068 / ICPB 4128) (Pirella
OS staleyi).
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Pirellula.
OX NCBI_TaxID=530564 {ECO:0000313|EMBL:ADB18736.1, ECO:0000313|Proteomes:UP000001887};
RN [1] {ECO:0000313|EMBL:ADB18736.1, ECO:0000313|Proteomes:UP000001887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27377 / DSM 6068 / ICPB 4128
RC {ECO:0000313|Proteomes:UP000001887};
RX PubMed=21304671; DOI=10.4056/sigs.51657;
RA Clum A., Tindall B.J., Sikorski J., Ivanova N., Mavrommatis K., Lucas S.,
RA Glavina del Rio T., Nolan M., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA Goodwin L., Ovchinikova G., Pati A., Mikhailova N., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Pirellula staleyi type strain (ATCC 27377).";
RL Stand. Genomic Sci. 1:308-316(2009).
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 -!- 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; CP001848; ADB18736.1; -; Genomic_DNA.
DR AlphaFoldDB; D2R303; -.
DR STRING; 530564.Psta_4086; -.
DR KEGG; psl:Psta_4086; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_4_0; -.
DR Proteomes; UP000001887; 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:SF15; FORMATE DEHYDROGENASE H; 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 Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW Reference proteome {ECO:0000313|Proteomes:UP000001887}.
FT DOMAIN 56..112
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 764 AA; 84967 MW; 3EA40D0ACB62BFAD CRC64;
MIKLLPLLQM IHLDDAPRAS HENSLLRTWD GPLTRELSLQ NEQLGLPLLP QRLAPETTTT
MVCGFCSTGC GLKIHLRDGE AINVSPDTSY PVNLGMACPK GWEGLAPLSA PDRATTPLFR
DQSTGEFRPI DWHQAAEHFR NQFQSIQAKY GPESVAFLST GQIATEEMFL LGAVAKFGFG
FLHGDSNTRQ CMATAATAYK QSLGFDAPPY TYSDFEESDL LVFVGANPCI AHPILWERVL
ANRRQAKIVV IDPRQSETAQ AAHMHLAIRP KSDQTFFYGI TRLLIERGWM DRDYIEQHTS
GYAEFQAFLE AFTLERLQLE TGLTLSQIEG FARLVHQSER TSFWWTMGVN QSYQGVRTAQ
SIINLALVTG NFGRPGTGAN SITGQCNAMG SRLFSNTSAL AGGRDFTRED HRHEVAKILG
IDAARIPSSS GMAYDEILDA VRAGKIRGLW IIATNTAHSW IEQAETRQAL AQLDFLVVQD
IYTTTETAQL AHLILPAAPW GEKEGTFINS ERRVGRIKRV QRSPGSALAD FSIFRLLAKY
WGGLEQFEEL DSPAKVFAVL QELSRGRPCD ITGIRGYQHL DEAGGIQWPW TESDAAAASR
FSERPMPIGS QQRRLFSEGK FFHPDGRAKL LFDAPRPMPE QPNAEFPLLL LTGRGSVAQW
HTQTRTSKSA VLRKLYPADL YIEIHPEDAE RLGITHACAV RVRSRRATIV ARTCVVTTVA
PGTIFAPMHY AAVNQLTLAH YDPHSRQPSY KDCAVRVDRM GEGL
//
