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Database: UniProt
Entry: A6GRB8_9BURK
LinkDB: A6GRB8_9BURK
Original site: A6GRB8_9BURK 
ID   A6GRB8_9BURK            Unreviewed;       818 AA.
AC   A6GRB8;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Nitrite reductase (NAD(P)H) large subunit, NirB {ECO:0000313|EMBL:EDM83391.1};
GN   ORFNames=LMED105_07313 {ECO:0000313|EMBL:EDM83391.1};
OS   Limnobacter sp. MED105.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Limnobacter.
OX   NCBI_TaxID=391597 {ECO:0000313|EMBL:EDM83391.1, ECO:0000313|Proteomes:UP000010322};
RN   [1] {ECO:0000313|EMBL:EDM83391.1, ECO:0000313|Proteomes:UP000010322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED105 {ECO:0000313|EMBL:EDM83391.1,
RC   ECO:0000313|Proteomes:UP000010322};
RA   Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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:EDM83391.1}.
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DR   EMBL; ABCT01000008; EDM83391.1; -; Genomic_DNA.
DR   RefSeq; WP_008250586.1; NZ_ABCT01000008.1.
DR   AlphaFoldDB; A6GRB8; -.
DR   STRING; 391597.LMED105_07313; -.
DR   OrthoDB; 9768666at2; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000010322; 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   Gene3D; 3.90.480.10; Sulfite Reductase Hemoprotein;Domain 2; 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:UP000010322}.
FT   DOMAIN          9..290
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          324..391
FT                   /note="NADH-rubredoxin oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18267"
FT   DOMAIN          428..475
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          492..542
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          567..629
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          637..773
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
SQ   SEQUENCE   818 AA;  89326 MW;  0B5F1326F6A3D509 CRC64;
     MLMSVKKQKL VVIGNGMAGI RVVEELIKLA PDLYEITVFG AEPHPNYNRI MLSPVLAGEQ
     KFEEIVLNDW DWYTSNNITL HVGREVTEID RVKRLVKCAD GTTAPYDRLL LATGSNSFIL
     PVPGSTLPGV IGYRDIADTE AMLEAAKHYK KAIVIGGGLL GLEAANGLAI QGMDVSVVHL
     PTWLMERQLD PTAAGLLQKS LETKGLKFLL AKNTKALHAG ADGRVAKIEF ADGEVHDADL
     VVMAVGIRPN DKLAASSGLH CNRGVVVNDT MQTITDPKIY SVGECASHRG VAYGLVAPLF
     EQAKVCANHL AQFGIGRYEG SVTSTKLKVT GVDLFSAGNF MGGEGCEELL LSDPIGGVYK
     KLVIKEDKLV GACLYGDTVD GSWYFKLMRE GKAIKEIREK LMFGQNNIGD TGHEGQSQAS
     KMLDTDEVCG CNGVCKGTIV QAIKTKGLFT IEEVRKHTKA SASCGSCTGL CEQILMSTAG
     ADYSATPKTK PMCGCTDHGH QVVRDAIFKH HLTTKEEVFA TMNWRTPNGC ASCRPAVNYY
     LISSWPGEAV DDPQSRFINE RAHANIQKDK TYSVVPRMWG GETTAAELRR IADVVDKYNI
     PTVKVTGGQR IDLLGVKKED LQDVWKDLDM PSGHAYAKGL RTVKTCVGSE WCRFGTQDST
     QMGKDLERGL FKMYAPHKVK LAVSGCPRNC AESGIKDVGV IGVDSGWEIY VGGNGGIKTE
     VAQFLCRVKT SDEVMAVSGA FLQLYRKEGW YLERTVHYLE RVGLEHAKAR VVDDVANRNA
     LWAELQAALA IEEDPWHKPK EAQVDLRQFI PIKLAEVV
//
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