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Database: UniProt
Entry: A0A074J4S8_9RHOB
LinkDB: A0A074J4S8_9RHOB
Original site: A0A074J4S8_9RHOB 
ID   A0A074J4S8_9RHOB        Unreviewed;       816 AA.
AC   A0A074J4S8;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Nitrite reductase {ECO:0000313|EMBL:KEO51519.1};
GN   ORFNames=TP2_11535 {ECO:0000313|EMBL:KEO51519.1};
OS   Thioclava pacifica DSM 10166.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Thioclava.
OX   NCBI_TaxID=1353537 {ECO:0000313|EMBL:KEO51519.1, ECO:0000313|Proteomes:UP000027432};
RN   [1] {ECO:0000313|EMBL:KEO51519.1, ECO:0000313|Proteomes:UP000027432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10166 {ECO:0000313|EMBL:KEO51519.1,
RC   ECO:0000313|Proteomes:UP000027432};
RA   Lai Q., Shao Z.;
RT   "Thioclava pacifica DSM 10166 Genome Sequencing.";
RL   Submitted (JUL-2013) 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:KEO51519.1}.
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DR   EMBL; AUND01000038; KEO51519.1; -; Genomic_DNA.
DR   RefSeq; WP_038078887.1; NZ_AUND01000038.1.
DR   AlphaFoldDB; A0A074J4S8; -.
DR   STRING; 1353537.TP2_11535; -.
DR   eggNOG; COG1251; Bacteria.
DR   OrthoDB; 9768666at2; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000027432; 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:UP000027432}.
FT   DOMAIN          7..287
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          319..384
FT                   /note="NADH-rubredoxin oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18267"
FT   DOMAIN          422..470
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          484..533
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          559..622
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          633..769
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
SQ   SEQUENCE   816 AA;  88806 MW;  AB8E274AC8DFCB0B CRC64;
     METQKQKLVI IGNGMAPGRM LEHLFDLTDA YEVTIFNAEP RVNYDRIMLS PVLSGEKSYA
     DIIIHGEGWY EEHGITLHMG EKVVGIDRVE RKVTSDKGTV EHYDKLVIAT GSQPFIIPVP
     GKDLPGVLAY RDLDDTEAMI SAADKGGKAV VIGGGLLGLE AAAGLRLRGM DVTVLHLMPS
     LMERQLDEAS GYLLQRALEA RGIDVKCRAN TKAILGTDKV EGVELEDGSV LEADLVVMAV
     GIRPNSGLAK EAGIEVNRGI VTDATMRTSD HAIYALGECA EVDGRVYGLV APLYEMAKVA
     AHALAGEETA GFKHSETPTK LKVTGCDLYS VGDFAEGEGR EDIVLRDAQR GSYKRVILKD
     NKIIGAVLYG DVADGGWFNE MLRAGTDVSD MRETLIFGQA HQGGGSFDPV AAAAALPDDA
     EICGCNGICK GQIVQAITDK GLTALSEVRA HTKASASCGT CANNVENLLK AVLGDAFEKK
     AEGMCGCTPL GHGEVRRLIK ANHLKSIPEV MQELEWSSPE GCAKCRPALN YYLVSDWPGE
     YEDDYRSRFI NERVHANIQK DGTYSVVPRI WGGKTTAAEL RAIADIAEKY NVPEVKFTGG
     QRIDLLGIKK EDLPGIWADL NEHGMVSGGA YTKGLRTVKT CVGQEWCRFG TQDSMGLGVK
     LEKFLWGSWT PAKLKLAVTG CPRNCAEATC KDIGIICVDS GYQIVYGGAA GLHIQGTTEL
     GTVATEEEVI EITAAITQLY REEGFYLERI YKWADRVGYD RIKSIVLEDK EARRELHDRF
     VFSQKFAQVD PWAERVAGKD AHEFKPMAEF KLEAAE
//
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