ID C7PXU1_CATAD Unreviewed; 830 AA.
AC C7PXU1;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:ACU73401.1};
GN OrderedLocusNames=Caci_4538 {ECO:0000313|EMBL:ACU73401.1};
OS Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS B-24433 / ID139908).
OC Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC Catenulisporaceae; Catenulispora.
OX NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU73401.1, ECO:0000313|Proteomes:UP000000851};
RN [1] {ECO:0000313|EMBL:ACU73401.1, ECO:0000313|Proteomes:UP000000851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908
RC {ECO:0000313|Proteomes:UP000000851};
RX PubMed=21304647; DOI=10.4056/sigs.17259;
RA Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT 139908).";
RL Stand. Genomic Sci. 1:119-125(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 -!- 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; CP001700; ACU73401.1; -; Genomic_DNA.
DR RefSeq; WP_015793130.1; NC_013131.1.
DR AlphaFoldDB; C7PXU1; -.
DR STRING; 479433.Caci_4538; -.
DR KEGG; cai:Caci_4538; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_4_11; -.
DR InParanoid; C7PXU1; -.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000000851; 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; 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; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 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:UP000000851}.
FT DOMAIN 41..97
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 785..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 830 AA; 90137 MW; E34CE8D45A22A93E CRC64;
MALVDRIAQP WGERTPYRPG QPWPARVDTF LDSGVQESQV QRWARSASLL HSNGDAMDIA
VADGRIVGVR GRAADRVNRG RLGPKDLYGW QANNSPDRLT APLIRQDGRL VECGWDTAMQ
RIAERSRQLL ESHGPGAIGF YTTGQLFLEE YYTLTVIARA GIGTNHLDGN TRLCTATAGE
ALKESFGCDG QPGSFTDVDH ADVIALYGHN VAETQPVLWM RMLDRLDGPE PPRLLVVDPR
RTVPAERAAV HLAPRPGTNL ALMNALVHEV IRRGAVARDF VRDHAIGFDD LAAAVADCTP
DWAAAICDVP AAAIGRAAEL IAGAEKLTST VLQGFYQSHQ ATAAAVQVNN LHVLRGMLGR
PGCGVLQMNG QPTAQNTREC GANGDLPGFR NWANAEHVAE LADLWNVEAE QIPHWGPPTH
AMQMLRYAEQ GSIKMLWISG TNPAVSLPDL HRVRSVLSQE RLFTVVQDIF LTETAELADV
VLPAATWGEK TGCFTNADRT VHLSEKAVDP PGAARPDLDI FLDYAQRMEL RDKDGQPLIA
WTDAEGAFEA WKACSAGRLC DYTGLSHGRL RQEPSGIQWP CTEDRPQGTE RLYSDGQFWA
RPAEAETYGK DLETGAAFTE SDYRAWNPEG RSLLRSAVYF PAPEVPDEEF PLWLTTGRTL
YHFHTRTKTA RAPQLNRAAP EVWVEMSAGE AERRGLAEGD LAEISSARGR LRARVRVAHV
RDGVLFVPFH YGYFDVPGGP PDRRNQAGSA ANETTITAWD PASKQPLFKA CAARIAAVEG
AAVASAEASS APTTTASAPA GRSANLVPPT IGGPDALSTS TSTSTTTRQD
//
