ID Q63L49_BURPS Unreviewed; 1267 AA.
AC Q63L49;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE SubName: Full=Respiratory nitrate reductase subunit {ECO:0000313|EMBL:CAH38627.1};
DE EC=1.7.99.4 {ECO:0000313|EMBL:CAH38627.1};
GN Name=narG {ECO:0000313|EMBL:CAH38627.1};
GN OrderedLocusNames=BPSS1159 {ECO:0000313|EMBL:CAH38627.1};
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH38627.1, ECO:0000313|Proteomes:UP000000605};
RN [1] {ECO:0000313|EMBL:CAH38627.1, ECO:0000313|Proteomes:UP000000605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243 {ECO:0000313|EMBL:CAH38627.1,
RC ECO:0000313|Proteomes:UP000000605};
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M., Atkins T.,
RA Crossman L.C., Pitt T., Churcher C., Mungall K., Bentley S.D., Sebaihia M.,
RA Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F.,
RA Challis G.L., Cherevach I., Chillingworth T., Cronin A., Crosset B.,
RA Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H.,
RA Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S.,
RA Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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; BX571966; CAH38627.1; -; Genomic_DNA.
DR RefSeq; WP_011205550.1; NZ_CP009537.1.
DR RefSeq; YP_111172.1; NC_006351.1.
DR AlphaFoldDB; Q63L49; -.
DR STRING; 272560.BPSS1159; -.
DR KEGG; bps:BPSS1159; -.
DR PATRIC; fig|272560.51.peg.4384; -.
DR eggNOG; COG5013; Bacteria.
DR Proteomes; UP000000605; Chromosome 2.
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:UniProtKB-EC.
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 Gene3D; 4.10.1200.10; nitrate reductase tail; 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; IPR006468; NarG.
DR InterPro; IPR028189; Nitr_red_alph_N.
DR InterPro; IPR044906; Nitr_red_alph_N_sf.
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 Pfam; PF14710; Nitr_red_alph_N; 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; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:CAH38627.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000605}.
FT DOMAIN 43..107
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 1241..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1267 AA; 141094 MW; 70A89480A3BC8912 CRC64;
MSHFLDRLRF FTTTRPQFSD GHGAVTDEDR KWEEGYRQRW QHDKIVRSTH GVNCTGSCSW
KVYVKGGIVT WETQQTDYPR TRPDMPNHEP RGCSRGASYS WYLYSANRLK YPLVRSALVR
LWRERRRTMA PVDAWRSIVD DEHARRGYQS RRGLGGFVRA TWDEVDEIVA AANVHTVARH
GPDRVVGFSP IPAMSMVSYA AGSRYLSLIG GVCLSFYDWY CDLPPASPQT WGEQTDVPES
ADWYNSTFIM MWGSNVPQTR TPDAHFLVEA RYRGTKIVSV FPDYSEGAKF GDLWLHPKQG
TDAALALAMG HVILKEFHVD GASDYFSDYC RRYTDMPCIV RLVPHGAGYV PERLVRASDF
DGALGEAEHP EWKTVMIDDA TGEFVVPVGS IGFRWAQPGG GDRGKWNLKE QTSRGAALAP
RLSLASAHDE VVDVLFPYFG NQPHAHFAPT PHAGELSRRI GARRVTTPGG EMLVATVYDL
FVANYGIDQG LGGRDVATSY DDDVPYTPAW QEAITGVKRE DAISVARQFA QNAHKTQGKS
MVIVGAGINH WFHMDMTYRA IINMLIMCGC VGKSGGGWSH YVGQEKLRPQ TGWTALAFAL
DWHRPPRQMN ATSFFYAHTD QWRYDPMDPA ALLSPLADKS RFHGAPIDYN VRAERMGWLP
CAPQLAANPL RVGADIADPA HAGAEIARRL ASGELKMACE DPDAPENFPR NLFVWRSNLL
GSSGKGHEYF LKHLLGTAHG VQGDEIREGG GVRRPEEVTW HADAPRGKLD LLVTLDFRMS
TTCMYSDVVL PTATWYEKDD MNTSDMHPFI HPLSAAVDPA WQSKSDWEIF KGIAKRFSEL
AEGHLGIERD VVLAPIAHDS AAELAQPFDV RDWKRGECDA VPGRTMPAVT VVDRDYPSTY
RKYTSLGPLM ERLGNGGKGI GWDAKDEVAL LGALNYRVTE AGCAQGRPRI DSALDAAEVI
LALAPETNGA VAVKAWQALS AITGLEHAHL ARAREDEKIR FRDLQAQPRK IISSPTWSGI
ESEHVSYNAG YVNVHELVPW RTLSGRQQLY QDHPWMRAFG EALCAYKPPI DTGSYAHMVG
QRSNGHPEIV LNFITPHQKW GIHSTYTDNL LMLTLSRGGP IVWISERDAQ AIGVVDNDWI
ECYNANGALC ARAVVSQRVP RGMVMMYHAQ EKIVNTPGSE ITGTRGGIHN SVTRVSLKPT
HMIGGYAQLS YGFNYYGTVG SNRDEFLIVR KMKRIDWLDG ENESARAPSV STSGADDERH
ADAGETR
//
