ID F3KRS2_9BURK Unreviewed; 827 AA.
AC F3KRS2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Nitrite reductase (NAD(P)H) large subunit {ECO:0000313|EMBL:EGI77523.1};
GN ORFNames=HGR_05601 {ECO:0000313|EMBL:EGI77523.1};
OS Hylemonella gracilis ATCC 19624.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hylemonella.
OX NCBI_TaxID=887062 {ECO:0000313|EMBL:EGI77523.1, ECO:0000313|Proteomes:UP000016368};
RN [1] {ECO:0000313|EMBL:EGI77523.1, ECO:0000313|Proteomes:UP000016368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19624 {ECO:0000313|EMBL:EGI77523.1,
RC ECO:0000313|Proteomes:UP000016368};
RX PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA Jensen G.J.;
RT "Structural diversity of bacterial flagellar motors.";
RL EMBO J. 30:2972-2981(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRNR:PIRNR037149};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- COFACTOR:
CC Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC Evidence={ECO:0000256|ARBA:ARBA00001929};
CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC {ECO:0000256|ARBA:ARBA00005096}.
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000256|ARBA:ARBA00010429}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGI77523.1}.
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DR EMBL; AEGR01000045; EGI77523.1; -; Genomic_DNA.
DR RefSeq; WP_006297126.1; NZ_AEGR01000045.1.
DR AlphaFoldDB; F3KRS2; -.
DR STRING; 887062.HGR_05601; -.
DR eggNOG; COG1251; Bacteria.
DR OrthoDB; 9768666at2; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000016368; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniRule.
DR CDD; cd19943; NirB_Fer2_BFD-like_1; 1.
DR CDD; cd19944; NirB_Fer2_BFD-like_2; 1.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 1.
DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR InterPro; IPR012744; Nitri_red_NirB.
DR InterPro; IPR017121; Nitrite_Rdtase_lsu.
DR InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR InterPro; IPR041575; Rubredoxin_C.
DR NCBIfam; TIGR02374; nitri_red_nirB; 1.
DR PANTHER; PTHR43809; NITRITE REDUCTASE (NADH) LARGE SUBUNIT; 1.
DR PANTHER; PTHR43809:SF1; NITRITE REDUCTASE (NADH) LARGE SUBUNIT; 1.
DR Pfam; PF04324; Fer2_BFD; 2.
DR Pfam; PF01077; NIR_SIR; 1.
DR Pfam; PF03460; NIR_SIR_ferr; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF18267; Rubredoxin_C; 1.
DR PIRSF; PIRSF037149; NirB; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 1.
DR SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 1.
DR PROSITE; PS00365; NIR_SIR; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR037149};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR037149}; Heme {ECO:0000256|ARBA:ARBA00022617};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063,
KW ECO:0000256|PIRNR:PIRNR037149};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000016368}.
FT DOMAIN 5..289
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 324..393
FT /note="NADH-rubredoxin oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18267"
FT DOMAIN 431..478
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
FT DOMAIN 496..549
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
FT DOMAIN 575..636
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 645..781
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
SQ SEQUENCE 827 AA; 90680 MW; 19FB1945A834F698 CRC64;
MKKMNLVMIG NGMAGVRSLE ELIKLAPELY NITVFGAEPH PNYNRILLSP VLAGEQQLED
IVLNDWAWYE TNGITLHAGW TVTEIDRQQR LVHARNAQGE TRSAPYDRLI LATGSKPFIL
PVPGKDLQGV LAYRDIADTE AMIAAAAQYK NAVVIGGGLL GLEAANGLMK RGMDVTVVHV
APWLMERQLD EVAGRMLQKS LEDRGMTFRI GAQTQELLGD ANGRVAHVRF QNGEELPADL
VVMAVGIRPN TTLAEQTGLH VNRGIVVNDT LQTTTDPRIY AVGECAAHRG IAYGLVAPLF
EQGKVLANHL AQFGIGRYTG SLTSTKLKVT GIDLFSAGDF LGGPGTEEIV LSDPHAEGGG
VYKKLVLKDD KLVGACLYGD TVDGSWYFKL LRDGRNVSDL RDKLMFGESN IGDAGHQGQS
RAMAMADSDE VCGCNGVTKG TICKAIKEKG LFTLDDVRKH TKASASCGSC TGLVEQILMF
TAGGDYSATP KTKALCACTE HGHQAVRDAI RTPLPDGGKL LTIPDVYRHL NWKTPNGCAT
CRPAVNYYLL STWPKEAQDD PQSRYINERS HANIQKDGTY SVVPRMWGGE TTADELRRIA
NAVDKYKIPT VKVTGGQRID LLGVKKEDLQ AVWRDIGMPS GHAYAKALRT VKTCVGSEWC
RMGTQDSTQM GKDLERALWR MQAPHKVKLA VSGCPRNCAE SGIKDVGVIG VDSGWELHIA
GNGGIKTEVA QFLCKVKTAA EVLEYSGAFL QLYREEGWYL ERTVHYVGRV GLDYVKKKIL
DDHEGRRALW ERLQYTLDGE PDPWFEADKA RVDQRQFIPI KVEKTTA
//
