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-MAY-2013, entry version 41.
DE RecName: Full=Periplasmic nitrate reductase;
DE EC=1.7.99.4;
DE Flags: Precursor;
GN Name=napA; 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 (By similarity).
CC -!- CATALYTIC ACTIVITY: Nitrite + acceptor = nitrate + reduced
CC acceptor.
CC -!- COFACTOR: Binds 1 4Fe-4S cluster (By similarity).
CC -!- COFACTOR: Binds 1 molybdenum ion per subunit (By similarity).
CC -!- COFACTOR: Binds 2 molybdopterin guanine dinucleotide (MGD) groups
CC per subunit (By similarity).
CC -!- SUBUNIT: Interacts with NapB (By similarity).
CC -!- SUBCELLULAR LOCATION: Periplasm (By similarity).
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.
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DR EMBL; CP001013; ACB33611.1; -; Genomic_DNA.
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; HWIKAAR; -.
DR ProtClustDB; PRK13532; -.
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-KW.
DR GO; GO:0009055; F:electron carrier activity; IEA:HAMAP.
DR GO; GO:0005506; F:iron ion binding; IEA:HAMAP.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0008940; F:nitrate reductase activity; IEA:HAMAP.
DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:HAMAP.
DR GO; GO:0042128; P:nitrate assimilation; IEA:HAMAP.
DR Gene3D; 2.40.40.20; -; 1.
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_Fe4S4_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
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; Asp_decarb_fold; 1.
DR TIGRFAMs; TIGR01706; NAPA; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; FALSE_NEG.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; FALSE_NEG.
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; Signal; Transport.
FT SIGNAL 1 29 Tat-type signal (Potential).
FT CHAIN 30 851 Periplasmic nitrate reductase.
FT /FTId=PRO_5000331867.
FT METAL 51 51 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 54 54 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 58 58 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 86 86 Iron-sulfur (4Fe-4S) (By similarity).
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
//
