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Database: UniProt
Entry: B1Y6A6
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ID   NAPA_LEPCP              Reviewed;         851 AA.
AC   B1Y6A6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   01-OCT-2014, entry version 50.
DE   RecName: Full=Periplasmic nitrate reductase {ECO:0000255|HAMAP-Rule:MF_01630};
DE            EC=1.7.99.4 {ECO:0000255|HAMAP-Rule:MF_01630};
DE   Flags: Precursor;
GN   Name=napA {ECO:0000255|HAMAP-Rule:MF_01630};
GN   OrderedLocusNames=Lcho_1343;
OS   Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS   discophora (strain SP-6)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Leptothrix.
OX   NCBI_TaxID=395495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51168 / LMG 8142 / SP-6;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT   "Complete sequence of Leptothrix cholodnii SP-6.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalytic subunit of the periplasmic nitrate reductase
CC       (NAP). Only expressed at high levels during aerobic growth. NapAB
CC       complex receives electrons from the membrane-anchored tetraheme
CC       protein NapC, thus allowing electron flow between membrane and
CC       periplasm. Essential function for nitrate assimilation and may
CC       have a role in anaerobic metabolism. {ECO:0000255|HAMAP-
CC       Rule:MF_01630}.
CC   -!- CATALYTIC ACTIVITY: Nitrite + acceptor = nitrate + reduced
CC       acceptor. {ECO:0000255|HAMAP-Rule:MF_01630}.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster. {ECO:0000255|HAMAP-
CC       Rule:MF_01630}.
CC   -!- COFACTOR: Binds 1 molybdenum-bis(molybdopterin guanine
CC       dinucleotide) (Mo-bis-MGD) cofactor per subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_01630}.
CC   -!- SUBUNIT: Interacts with NapB. {ECO:0000255|HAMAP-Rule:MF_01630}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01630}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of
CC       the signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. NasA/NapA/NarB subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01630}.
CC   -!- SIMILARITY: Contains 1 4Fe-4S Mo/W bis-MGD-type domain.
CC       {ECO:0000255|HAMAP-Rule:MF_01630}.
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DR   EMBL; CP001013; ACB33611.1; -; Genomic_DNA.
DR   RefSeq; WP_012346373.1; NC_010524.1.
DR   RefSeq; YP_001790376.1; NC_010524.1.
DR   ProteinModelPortal; B1Y6A6; -.
DR   SMR; B1Y6A6; 43-848.
DR   STRING; 395495.Lcho_1343; -.
DR   EnsemblBacteria; ACB33611; ACB33611; Lcho_1343.
DR   GeneID; 6160329; -.
DR   KEGG; lch:Lcho_1343; -.
DR   PATRIC; 22392985; VBILepCho83238_1345.
DR   eggNOG; COG0243; -.
DR   HOGENOM; HOG000031441; -.
DR   KO; K02567; -.
DR   OMA; CACKVER; -.
DR   OrthoDB; EOG6CVV7G; -.
DR   BioCyc; LCHO395495:GHYL-1361-MONOMER; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009055; F:electron carrier activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0008940; F:nitrate reductase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01630; Nitrate_reduct; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR   InterPro; IPR010051; Periplasm_NO3_reductase_lsu.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
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   TIGRFAMs; TIGR01706; NAPA; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Molybdenum; Nitrate assimilation; Oxidoreductase;
KW   Periplasm; Reference proteome; Signal; Transport.
FT   SIGNAL        1     29       Tat-type signal. {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   CHAIN        30    851       Periplasmic nitrate reductase.
FT                                /FTId=PRO_5000331867.
FT   DOMAIN       44    100       4Fe-4S Mo/W bis-MGD-type.
FT                                {ECO:0000255|HAMAP-Rule:MF_01630}.
FT   METAL        51     51       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   METAL        54     54       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   METAL        58     58       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
FT   METAL        86     86       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01630}.
SQ   SEQUENCE   851 AA;  94789 MW;  30900AA43A5B5A76 CRC64;
     MQSNRRDFLK AQALAASAAA AGIPIVVEAA NGTAAPKTAA DVAVRWDKAP CRFCGTGCAV
     MVGVQEGKVV ATQGDPEAPV NRGLNCIKGY FLSKIMYGRD RLQTPLLRKK NGVYDKEGDF
     VPVSWDEAFD IMAAKWKETL KTDGPTGIGM FGSGQWTVWE GYAAAKLWKA GFRSNNLDPN
     ARHCMASAVT GFMRTFGIDE PMGCYDDIEQ SDAFVLWGSN MAEMHPILWS RITDRRLSNP
     HVKVAVLSTY EHRSFDLADQ AMIFKPQTDL AILNYIANYI ITNKKVNTEF VKKNINFKKG
     ATDIGYGLRP GHALEKDATS NGYPGADGKP KGNPNDSTPI SFDEYAKFVS EYTAEKVSEI
     SGVTVEQLKA LAELYADPKV KVVSYWTMGF NQHTRGTWAN NMVYNIHLLT GKISQPGNGP
     FSLTGQPSAC GTAREVGTFA HRLPADMVVT NPEHRHHAEE IWGLPEGTIP DKIGLHAVAQ
     SRALKDGKLK CYWVTTNNNM QAGPNINGEI LPGWRNPKTF IVVSDPYPTA SAMAADLVLP
     AAMWVEKEGA FGNAERRTQV WRQQVSAPGE ARSDLWQMME FSKRFKIEDV WTAELIAKKP
     AVKGKTLFDV LFRNGKVDKY PLADLTKVNA KYIKDYTNDE SKAYGFYVQK GLFEEYAEFG
     RGHGHDLAPF DVYHEVRGLR WPVVDGKETL WRFREGYDPY VKKGEGVKFY GHKDGRANIF
     ALPYQPAAES PDKEYDLWLC TGRVLEHWHT GTMTRRVPEL HRAVPEAQLF MHPDDAKARG
     LQRGMKVKIA SRRGEILLAV ETKGRNKVPR GLVFVPFFDE GKLINKLTLD ATCPISKETD
     FKKCAVKVVR A
//
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