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Periplasmic nitrate reductase (EC 1.9.6.1)

 A0A0G3DI27_CAMLA        Unreviewed;       924 AA.
A0A0G3DI27;
16-SEP-2015, integrated into UniProtKB/TrEMBL.
16-SEP-2015, sequence version 1.
23-MAY-2018, entry version 24.
RecName: Full=Periplasmic nitrate reductase {ECO:0000256|HAMAP-Rule:MF_01630};
EC=1.9.6.1 {ECO:0000256|HAMAP-Rule:MF_01630};
Name=napA {ECO:0000256|HAMAP-Rule:MF_01630};
ORFNames=CD56_05240 {ECO:0000313|EMBL:AKJ53749.1};
Campylobacter lari.
Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
Campylobacteraceae; Campylobacter.
NCBI_TaxID=201 {ECO:0000313|EMBL:AKJ53749.1, ECO:0000313|Proteomes:UP000035197};
[1] {ECO:0000313|Proteomes:UP000035197}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Slaughter Beach {ECO:0000313|Proteomes:UP000035197};
Meinersmann R.J., Lindsey R.L., Bono J.L., Loparev V.N.,
Genzlinger L.L., Oakley B.B.;
"Genome sequence of an urease-positive Campylobacter lari.";
Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalytic subunit of the periplasmic nitrate reductase
complex NapAB. Receives electrons from NapB and catalyzes the
reduction of nitrate to nitrite. {ECO:0000256|HAMAP-Rule:MF_01630,
ECO:0000256|SAAS:SAAS00983823}.
-!- CATALYTIC ACTIVITY: 2 ferrocytochrome + nitrate + 2 H(+) = 2
ferricytochrome + nitrite. {ECO:0000256|HAMAP-Rule:MF_01630,
ECO:0000256|SAAS:SAAS00950067}.
-!- SUBUNIT: Component of the periplasmic nitrate reductase NapAB
complex composed of NapA and NapB. {ECO:0000256|HAMAP-
Rule:MF_01630, ECO:0000256|SAAS:SAAS00983817}.
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|HAMAP-Rule:MF_01630,
ECO:0000256|SAAS:SAAS00630820}.
-!- PTM: Predicted to be exported by the Tat system. The position of
the signal peptide cleavage has not been experimentally proven.
{ECO:0000256|HAMAP-Rule:MF_01630}.
-!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
oxidoreductase family. NasA/NapA/NarB subfamily.
{ECO:0000256|SAAS:SAAS00646089}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01630}.
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EMBL; CP011372; AKJ53749.1; -; Genomic_DNA.
RefSeq; WP_047208408.1; NZ_CP011372.1.
EnsemblBacteria; AKJ53749; AKJ53749; CD56_05240.
PATRIC; fig|201.18.peg.1035; -.
Proteomes; UP000035197; Chromosome.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
GO; GO:0050140; F:nitrate reductase (cytochrome) activity; IEA:UniProtKB-EC.
GO; GO:0008940; F:nitrate reductase activity; IEA:UniProtKB-UniRule.
GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniRule.
HAMAP; MF_01630; Nitrate_reduct_NapA; 1.
InterPro; IPR009010; Asp_de-COase-like_dom_sf.
InterPro; IPR006657; MoPterin_dinucl-bd_dom.
InterPro; IPR006656; Mopterin_OxRdtase.
InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
InterPro; IPR010051; Periplasm_NO3_reductase_lsu.
InterPro; IPR006311; TAT_signal.
InterPro; IPR019546; TAT_signal_bac_arc.
PANTHER; PTHR11615:SF123; PTHR11615:SF123; 2.
Pfam; PF04879; Molybdop_Fe4S4; 1.
Pfam; PF00384; Molybdopterin; 1.
Pfam; PF01568; Molydop_binding; 1.
SMART; SM00926; Molybdop_Fe4S4; 1.
SUPFAM; SSF50692; SSF50692; 1.
TIGRFAMs; TIGR01706; NAPA; 1.
TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
PROSITE; PS51318; TAT; 1.
3: Inferred from homology;
4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01630,
ECO:0000256|SAAS:SAAS00495824}; Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000035197};
Electron transport {ECO:0000256|HAMAP-Rule:MF_01630,
ECO:0000256|SAAS:SAAS00646091};
Iron {ECO:0000256|HAMAP-Rule:MF_01630, ECO:0000256|SAAS:SAAS00495824};
Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01630,
ECO:0000256|SAAS:SAAS00495824};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01630,
ECO:0000256|SAAS:SAAS00495824};
Molybdenum {ECO:0000256|HAMAP-Rule:MF_01630,
ECO:0000256|SAAS:SAAS00648831};
Nitrate assimilation {ECO:0000256|HAMAP-Rule:MF_01630,
ECO:0000256|SAAS:SAAS00646083};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01630,
ECO:0000256|SAAS:SAAS00509324};
Periplasm {ECO:0000256|HAMAP-Rule:MF_01630};
Signal {ECO:0000256|HAMAP-Rule:MF_01630, ECO:0000256|SAM:SignalP};
Transport {ECO:0000256|HAMAP-Rule:MF_01630,
ECO:0000256|SAAS:SAAS00646091}.
SIGNAL 1 29 {ECO:0000256|SAM:SignalP}.
CHAIN 30 924 Periplasmic nitrate reductase.
{ECO:0000256|SAM:SignalP}.
/FTId=PRO_5008835854.
DOMAIN 35 91 4Fe-4S Mo/W bis-MGD-type.
{ECO:0000259|PROSITE:PS51669}.
REGION 209 216 Mo-bis(molybdopterin guanine
dinucleotide) binding.
{ECO:0000256|HAMAP-Rule:MF_01630}.
REGION 552 553 Mo-bis(molybdopterin guanine
dinucleotide) binding.
{ECO:0000256|HAMAP-Rule:MF_01630}.
REGION 814 823 Mo-bis(molybdopterin guanine
dinucleotide) binding.
{ECO:0000256|HAMAP-Rule:MF_01630}.
COILED 390 410 {ECO:0000256|SAM:Coils}.
METAL 42 42 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
Rule:MF_01630}.
METAL 45 45 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
Rule:MF_01630}.
METAL 49 49 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
Rule:MF_01630}.
METAL 77 77 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
Rule:MF_01630}.
BINDING 79 79 Mo-bis(molybdopterin guanine
dinucleotide). {ECO:0000256|HAMAP-
Rule:MF_01630}.
BINDING 147 147 Mo-bis(molybdopterin guanine
dinucleotide). {ECO:0000256|HAMAP-
Rule:MF_01630}.
BINDING 172 172 Mo-bis(molybdopterin guanine
dinucleotide). {ECO:0000256|HAMAP-
Rule:MF_01630}.
BINDING 176 176 Mo-bis(molybdopterin guanine
dinucleotide). {ECO:0000256|HAMAP-
Rule:MF_01630}.
BINDING 417 417 Mo-bis(molybdopterin guanine
dinucleotide); via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01630}.
BINDING 421 421 Mo-bis(molybdopterin guanine
dinucleotide). {ECO:0000256|HAMAP-
Rule:MF_01630}.
BINDING 527 527 Mo-bis(molybdopterin guanine
dinucleotide); via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01630}.
BINDING 575 575 Mo-bis(molybdopterin guanine
dinucleotide). {ECO:0000256|HAMAP-
Rule:MF_01630}.
BINDING 602 602 Mo-bis(molybdopterin guanine
dinucleotide). {ECO:0000256|HAMAP-
Rule:MF_01630}.
BINDING 890 890 Substrate; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01630}.
BINDING 898 898 Mo-bis(molybdopterin guanine
dinucleotide). {ECO:0000256|HAMAP-
Rule:MF_01630}.
BINDING 915 915 Mo-bis(molybdopterin guanine
dinucleotide). {ECO:0000256|HAMAP-
Rule:MF_01630}.
SEQUENCE 924 AA; 104890 MW; A1EA110B9EAAECC8 CRC64;
MNRRDFIKNT AIASACGVAG LSVPSSVLAN TENKWRWDKA VCRFCGTGCG ILVASLDGKI
VAVKGDPAAP VNRGLNCIKG YFNAKIMYGE DRLVTPLLRV NVKGEFDKKG KFQQVSWQRA
FDEMEKQFKK AYKEKGAEGI GIFASGQYTI QEGYAAAKLV KAGFRSNNID PNARHCMASA
VVGFMQTFGV DEPSGCYDDI ELTDTIITWG ANMAEMHPIL WSRVSDRKLS NLDKVKIVNL
STFSNRTSHI ADTEIIFKPN TDLAIWNYIA REIVYNHPEA MDKEFIEKHC IFTTGYADIG
YGMRNNPNHP KFKASEKDTV AKQNAIIVDE EEAVSLAYLG VKAGDKFEMK HQNTPDAHWE
ISFEDFKKAL EPYTLDYVAK VAKGNEDESI EEFKKKLQEL ANLYIEKNRK VVSFWTMGFN
QHTRGTWVNE QAYMVHFLLG KQAKPGSGAF SLTGQPSACG TAREVGTFSH RLPADMVVAN
PKHREISEKI WKVPAKTINP KPGAPYLKIM RDLEDGNIKF AWVQVNNPWQ NTANANHWIA
AAREMDNFIV VSDCYPGISA KVADLILPSA MIYEKWGAYG NAERRTQHWK QQVLPVGEAM
SDTWQIMEFA KRFKLKEVWG ETKVNDKLTL PSVLEEAKAM GYSEDDTLYD VLFANKEAKS
FKAKDNIAKG FDNSEVFGDE RKVIGSDGKE FNGYGFFVQK YLWEEYRKFG LGHGHDLADF
DTYHKVRGLR WPVVNGKETQ WRFNTKFDYY AKKAAPNSDF AFYGDFAKEL PKGDLLAPQT
KEKYSLKNKV KIFFRPFMKA PERPSKEYPF WLCTGRVLEH WHSGTMTMRV PELFRAVPEA
LCYMNEDDAK AMKINQGDIV WVESRRGKVK ARVDFRGRNK PSKGLVYVPW FDENVYINKV
TLDATCPLSN QTDFKKCAVK ITKA


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