ID A0A387B8C4_9MICO Unreviewed; 862 AA.
AC A0A387B8C4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=assimilatory sulfite reductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012353};
DE EC=1.8.7.1 {ECO:0000256|ARBA:ARBA00012353};
GN ORFNames=D7I47_10180 {ECO:0000313|EMBL:AYF98593.1};
OS Protaetiibacter intestinalis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Protaetiibacter.
OX NCBI_TaxID=2419774 {ECO:0000313|EMBL:AYF98593.1, ECO:0000313|Proteomes:UP000278886};
RN [1] {ECO:0000313|Proteomes:UP000278886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2DFWR-13 {ECO:0000313|Proteomes:UP000278886};
RA Heo J., Kim S.-J., Kwon S.-W.;
RT "Genome sequencing of strain 2DFWR-13.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reduction of sulfite to sulfide, a step in the
CC biosynthesis of sulfur-containing amino acids and cofactors.
CC {ECO:0000256|ARBA:ARBA00003247}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 H2O + hydrogen sulfide + 6 oxidized [2Fe-2S]-[ferredoxin] =
CC 7 H(+) + 6 reduced [2Fe-2S]-[ferredoxin] + sulfite;
CC Xref=Rhea:RHEA:23132, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359,
CC ChEBI:CHEBI:29919, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.8.7.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000993};
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; CP032630; AYF98593.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A387B8C4; -.
DR KEGG; lyd:D7I47_10180; -.
DR OrthoDB; 9768666at2; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000278886; Chromosome.
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:0050311; F:sulfite reductase (ferredoxin) activity; IEA:UniProtKB-EC.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniRule.
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; 1.
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; 1.
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:UP000278886};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 9..292
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 325..389
FT /note="NADH-rubredoxin oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18267"
FT DOMAIN 423..475
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
FT DOMAIN 564..626
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 636..772
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT REGION 822..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 862 AA; 91736 MW; DFB3A8BFBA31878E CRC64;
MTERTPPRRV VVIGAGPAAH RLADAIRTRD AHGRIRLWVI GEEEHLPYDR VALSRRFLGG
DDLTLDASVW EHEAITLLRG ERAVAVDRVA RTVTTDAGRR LPYDDVVFAT GSRAPVPDIP
GAEHAHVYRT IADVEDLAAE VRLLAAVLGR PPRTVVAGGG LLGLEAAGGL AELGADSAIV
HSGGWLMSAQ LDEGAGQALG RLISARGITM HLGTRPREIR TTEGAVSAVK LTNGQTVPAD
LIVFAIGIAA RDELASAAAI ETAPRGGIVV DEECRASDPR VWAIGEVASV GGRCVGLVAP
ANAMAEVVAD RLLGGAAVFT TVDDATKLKL AGVEVASFGD AMGTSEGALE VVYADPARGM
YQKIVVSDDA RTLLGGVFVG DAAPYLTLRP MLGRELGSEP AAYLSASGAE PAGADELPDD
ALLCSCNNVT VGAVRKAVHG HDGQEACHTV PELKACTRAG LQCGSCVPLV KKTLEQELAK
AGLTVSHALC EHFAHSRQEL FELIRILGIS SWDDTLARFG TGRGCDICKP AVASILASQH
DGYVLDDGRG ALQDTNDRAL ANMQRDGSYS VVPRIPGGEI TPEKLGVIAR VATEFGLYTK
ITGGQRIDMF GARLDQLPDI WAQLVEAGFE SGQAYGKSLR NVKSCVGSTW CRFGVQDSVG
MAIRLELRYR GLRAPHKFKV GVSGCARECA EARGKDVGVI ATDAGWNLYV GGNGGFQPTH
AQLLASDLDD DTLIRFIDRY LMYYIRTADR LQRTARWMEE LDGGLDHVRA VVVDDSLGLG
AELESAMARH VEHYEDEWAA TLRDPERLKR FRSFLNAPGD AAPGIPRVSE RGQQRPATAA
ELREGKVMLA GARIPVRGDG DD
//
