ID Q1QHW9_NITHX Unreviewed; 1214 AA.
AC Q1QHW9;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN OrderedLocusNames=Nham_3449 {ECO:0000313|EMBL:ABE64178.1};
OS Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Nitrobacter.
OX NCBI_TaxID=323097 {ECO:0000313|EMBL:ABE64178.1, ECO:0000313|Proteomes:UP000001953};
RN [1] {ECO:0000313|EMBL:ABE64178.1, ECO:0000313|Proteomes:UP000001953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10229 / NCIMB 13809 / X14
RC {ECO:0000313|Proteomes:UP000001953};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L.,
RA O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T.,
RA Gentry M.E., Bruce D., Richardson P.;
RT "Complete sequence of chromosome of Nitrobacter hamburgensis X14.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + nitrate = a quinone + H2O + nitrite;
CC Xref=Rhea:RHEA:56144, ChEBI:CHEBI:15377, ChEBI:CHEBI:16301,
CC ChEBI:CHEBI:17632, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.7.5.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001854};
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP000319; ABE64178.1; -; Genomic_DNA.
DR RefSeq; WP_011511827.1; NC_007964.1.
DR AlphaFoldDB; Q1QHW9; -.
DR STRING; 323097.Nham_3449; -.
DR KEGG; nha:Nham_3449; -.
DR eggNOG; COG5013; Bacteria.
DR HOGENOM; CLU_000422_14_1_5; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000001953; Chromosome.
DR GO; GO:0009325; C:nitrate reductase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0008940; F:nitrate reductase activity; IEA:InterPro.
DR GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR GO; GO:0042126; P:nitrate metabolic process; IEA:InterPro.
DR CDD; cd02776; MopB_CT_Nitrate-R-NarG-like; 1.
DR CDD; cd02750; MopB_Nitrate-R-NarG-like; 1.
DR Gene3D; 3.40.50.12440; -; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037943; MopB_CT_Nitrate-R-NarG-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 InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006468; NarG.
DR NCBIfam; TIGR01580; narG; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR PANTHER; PTHR43105:SF2; RESPIRATORY NITRATE REDUCTASE 2 ALPHA CHAIN; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 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; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001953}.
FT DOMAIN 26..90
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1214 AA; 138544 MW; 12C3F7043200E663 CRC64;
MSWILDLVNP RERKWEEFYR NRWSHDNVFR STHGVNCTGG CSWAIYVKDG IITWEMQQTD
YPLLERSLPP YEPRGCQRGI SASWYVYSPI RVKYPYIRGP LLDMWREAKA SSADPVQAWG
ALIGDEQKRS RIQKARGKGG FRRAKWEELV ELIAAASLHT ARKHGPDRIM GFSPIPAMSM
LSFAAGTRFL SLMGGSLMSF YDWYADLPTS FPEIWGDQTD VCESADWYNS KFIVSMASNM
NMTRTPDVHF ISEARTEGTK FVVLSPDFSQ IAKYCDEWIP IQAGQDTALW MAANHVILKE
YYVDRQVPYF VDYIKRYTDL PFLVELESNG NTYKTGRLLR SNRVPRYKDV ENGDWKMLLL
DANSGELRAP KGQVGDRWGS VHGKWNLSGE DTLDNSPLDP VLSFIDRSDD VVQVGFDDFA
NGRIVSRGVP VKRVATDKGE ILCATGFDIM MSQFGISRGL EGAFATSYDD EDAPYTPAWQ
ERHTGIGRET AIRFAREFAT NAELTNGKSM VIVGASANHW YYNNLCYRSA TVALILCGCC
GVNGGGINHY VGQEKLAPVA PWATVALALD WAKPPRLVQS STWHYAHSCQ WRYEQEFTEY
GLTAPNPKWA KGHAIDLEAK AVHNGWMPFT PHFNRNPIEV AAEAERSGAK NVQDIETYVV
DQVVSKKLQM AIDDPDAAEN WPRMWFIWRG NAIQSSAKGH EFFLRHYLGA HDNAIAEDRA
KGKAQVVKYH ETAPRGKYDL VIDLNFRMNT TSLYSDIVLP TAFWYEKNDL NTTDLHSFLH
VLGQAVPPVW ESKTDWEIFK LIGKKVSELA PLAFSKPVRD VVLQPLMHDT PDELAQPEIL
DWSLGECKAV PGKSFPHVRV VERDYANLYN KFISFGPKAR EDGISAVGVQ IPIKKQYDQM
LDNPIMPMPD PRHMRCVEWG GKRYPSLEDV LDACNTVLLC APEANGEVCY QAFHNEEHHV
GLPLVDLAEP NRNVAATFYD LTRQPRRIIT SPCWTGMVND GRAYSAWCMN VERLVPWRTL
TGRQSLYLDH QWYLDFGEHI PTYKPRLNPR KTGDIVKSRV DDRSLVLNYI TPHGKWNIHS
TYKDNHRMLM LSRGMDPVWI NDRDAEKVGI EDNDWVEVYN DNGVVVTRAN VSRRIQPGTC
MYYHAVERTV YIPKSQERKW RGGGHNSLTR TRINPLFLAG GYAQFTYGWN YWGPTGILTR
DTHVVVRKME KLEW
//
