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NASC_BACSU
ID   NASC_BACSU              Reviewed;         710 AA.
AC   P42434;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 3.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Assimilatory nitrate reductase catalytic subunit;
DE            EC=1.7.-.-;
GN   Name=nasC; Synonyms=narB, nasBB; OrderedLocusNames=BSU03310;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA   Yamane K., Kumano M., Kurita K.;
RT   "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT   determination of the sequence of a 146 kb segment and identification of 113
RT   genes.";
RL   Microbiology 142:3047-3056(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION TO 391 AND 402.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-710.
RC   STRAIN=168;
RX   PubMed=7868621; DOI=10.1128/jb.177.5.1409-1413.1995;
RA   Ogawa K., Akagawa E., Yamane K., Sun Z.-W., Lacelle M., Zuber P.,
RA   Nakano M.M.;
RT   "The nasB operon and nasA gene are required for nitrate/nitrite
RT   assimilation in Bacillus subtilis.";
RL   J. Bacteriol. 177:1409-1413(1995).
RN   [5]
RP   INDUCTION BY TNRA.
RC   STRAIN=168;
RX   PubMed=10864496; DOI=10.1006/jmbi.2000.3846;
RA   Wray L.V. Jr., Zalieckas J.M., Fisher S.H.;
RT   "Purification and in vitro activities of the Bacillus subtilis TnrA
RT   transcription factor.";
RL   J. Mol. Biol. 300:29-40(2000).
RN   [6]
RP   INDUCTION BY TNRA.
RX   PubMed=12823818; DOI=10.1046/j.1365-2958.2003.03567.x;
RA   Yoshida K., Yamaguchi H., Kinehara M., Ohki Y.-H., Nakaura Y., Fujita Y.;
RT   "Identification of additional TnrA-regulated genes of Bacillus subtilis
RT   associated with a TnrA box.";
RL   Mol. Microbiol. 49:157-165(2003).
CC   -!- FUNCTION: Nitrate reductase is a key enzyme involved in the first step
CC       of nitrate assimilation in plants, fungi and bacteria.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250};
CC       Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC       bis-MGD) cofactor per subunit. {ECO:0000250};
CC   -!- PATHWAY: Nitrogen metabolism; nitrate reduction (denitrification);
CC       dinitrogen from nitrate: step 1/4.
CC   -!- INDUCTION: Positively regulated by TnrA under nitrogen-limited
CC       conditions. {ECO:0000269|PubMed:10864496, ECO:0000269|PubMed:12823818}.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; D50453; BAA08965.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12125.2; -; Genomic_DNA.
DR   EMBL; D30689; BAA06353.1; -; Genomic_DNA.
DR   PIR; E69665; E69665.
DR   RefSeq; NP_388213.2; NC_000964.3.
DR   RefSeq; WP_003246484.1; NZ_JNCM01000030.1.
DR   AlphaFoldDB; P42434; -.
DR   SMR; P42434; -.
DR   STRING; 224308.BSU03310; -.
DR   PaxDb; P42434; -.
DR   PRIDE; P42434; -.
DR   EnsemblBacteria; CAB12125; CAB12125; BSU_03310.
DR   GeneID; 938321; -.
DR   KEGG; bsu:BSU03310; -.
DR   PATRIC; fig|224308.179.peg.345; -.
DR   eggNOG; COG0243; Bacteria.
DR   InParanoid; P42434; -.
DR   OMA; GMNAHQH; -.
DR   PhylomeDB; P42434; -.
DR   BioCyc; BSUB:BSU03310-MON; -.
DR   UniPathway; UPA00652; UER00706.
DR   Proteomes; UP000001570; 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:0019333; P:denitrification pathway; IEA:UniProtKB-UniPathway.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
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   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
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; SSF50692; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE   2: Evidence at transcript level;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Molybdenum; Nitrate assimilation;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..710
FT                   /note="Assimilatory nitrate reductase catalytic subunit"
FT                   /id="PRO_0000063239"
FT   DOMAIN          19..77
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   BINDING         26
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   BINDING         29
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   BINDING         33
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   BINDING         63
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT   CONFLICT        391
FT                   /note="E -> D (in Ref. 1; BAA08965 and 4; BAA06353)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        402
FT                   /note="M -> V (in Ref. 1; BAA08965 and 4; BAA06353)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   710 AA;  78622 MW;  E9DDA80014D47A53 CRC64;
     MTERLLRYFR DKQQDVQSEK TYDTQCPFCS MQCKMQLVEQ TIVTRKKYTA IGIDNPTTQG
     RLCIKGMNAH QHALNSSRIT RPLLKKNGEF MPVSWEEALN HIKDQVTMIQ TEHGHDAMAV
     YGSASITNEE AYLLGKFARV GLQTKYIDYN GRLCMSAAAT AANQTFGADR GLTNPLSDIP
     HTRVIILAGT NIAECQPTIM PYFEKAKENG AYFIAIDPRE TATTKIADLH LKIKPGTDAA
     LANGLVKIII DEQLINEDFI QSRTNGFEEL KQHTDSLDLN DIAEQTSVSL VDIRKAAVKF
     AKETSGMLFT ARGIEQQTDG TAAVKGFLNM VLITGKIGKP YSGYGAITGQ GNGQGAREHG
     QKADQLPGYR SIENEEHRAH IAKVWGIHQD ELPRKGVSAY EMMEKINDGD IKGLFLMCSN
     PAVSSPNANL VKKALRRLTF FVAIDLFISE TAKYADVILP ASSYLEDEGT MTNVEGRVTL
     REASRPCPGE AKHDWQIICD LASALGKGRY FSYTSAEDIF NELREASRGG IADYSGISYG
     RLRREGGIHW PCPESDHPGT GRLFTESFAH PDQKAALSVI PNEPPVPKEK PTADYPLYLT
     TGRVMSHYLT GVQTRKSAAL AARHFESFME IHPQTAATYN IEDRVLVKIE SPRGSITVRS
     KLSEQIRKDT VFVPIHWADA QNVNDLIGEA LDPACKMPGF KVCAVRIIPI
 
 
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