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Database: UniProt
Entry: A0A286GLD1_9PROT
LinkDB: A0A286GLD1_9PROT
Original site: A0A286GLD1_9PROT 
ID   A0A286GLD1_9PROT        Unreviewed;       822 AA.
AC   A0A286GLD1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Assimilatory nitrite reductase (NAD(P)H) large subunit {ECO:0000313|EMBL:SOD96320.1};
GN   ORFNames=SAMN05421508_105267 {ECO:0000313|EMBL:SOD96320.1};
OS   Caenispirillum bisanense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Novispirillaceae; Caenispirillum.
OX   NCBI_TaxID=414052 {ECO:0000313|EMBL:SOD96320.1, ECO:0000313|Proteomes:UP000219621};
RN   [1] {ECO:0000313|EMBL:SOD96320.1, ECO:0000313|Proteomes:UP000219621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USBA 140 {ECO:0000313|EMBL:SOD96320.1,
RC   ECO:0000313|Proteomes:UP000219621};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) 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}.
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DR   EMBL; OCNJ01000005; SOD96320.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A286GLD1; -.
DR   OrthoDB; 9768666at2; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000219621; 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:UP000219621}.
FT   DOMAIN          15..292
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          327..393
FT                   /note="NADH-rubredoxin oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18267"
FT   DOMAIN          433..481
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          496..545
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          571..635
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          644..783
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
SQ   SEQUENCE   822 AA;  87333 MW;  0B864DE9D2F0163A CRC64;
     MTHVTHPAPG AAKPRLVVIG NGMAGIRAVE DLIDRAPGLY DITVFGAEPR VNYNRIMLSP
     LLSGEKTFAE IVLNDRDWYD ANGITLHAGD PVVRIDRLRR QVVARSGLAV PYDRLIVATG
     SSPIVIPVPG ATLPGVVTFR DVDDVDAMLD ASAKGGSAVV IGGGLLGLEA AVGLKARGMD
     VTVLHLAGHV MERQLDASAG HLLAEELRRR GLTVLTGADT AAILGDDRVT GVRLRDGTDI
     AADIVVMAVG IRPDARLAGE AGLDVERGVV VDDHMTTSDP AIFAVGECVQ HRGQCYGLVQ
     PLFEMAKVLG ARLAGLEGAG YVGSVTSTKL KVTGVDVFSA GDFSGGPGTE DIVFRDAGRG
     VYKRVVLQDG RVKGAVLYGD TADGAWYFQL LKAGEDVSDR RDTLLFGQAF AAAGAGTGNP
     TDAVAALPDD AEICGCNGVC KGTIVQAITT KGLTTLDEVK AHTKAAGSCG SCAGLVEGLL
     AHTLGGAYEA AAIKPLCKCT EHDHDSVRRL IKSQGLKSIP AVMQALEWKT PDGCASCRPA
     LNFYLLAAWP GEYVDHAASR FVNERVHANI QKDGTYSVVP RMWGGLTNAK ELRAIADVVD
     KFAIPTVKVT GGQRIDLLGI RKEDLPAVWA DLNAAGMVSG HAYGKSLRTV KTCVGSEWCR
     FGTQAAMSIG IDLERLTWGS WTPHKFKMAV SGCPRNCAEA TIKDFGVVAT DGGFDLYVGG
     NGGIKVRACD LLTKVTTEAE VHEYVGAFMQ LYREEARYLE RTAPWIERVG LDFVKKRIVE
     DAGNRAALNA RFLESQRHSQ SDPWAEQTQK HAASFKTLAT VE
//
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