ID A0A3G9IXN5_9ACTN Unreviewed; 846 AA.
AC A0A3G9IXN5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=assimilatory sulfite reductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012353};
DE EC=1.8.7.1 {ECO:0000256|ARBA:ARBA00012353};
GN ORFNames=Back2_14500 {ECO:0000313|EMBL:BBH17163.1};
OS Nocardioides baekrokdamisoli.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1804624 {ECO:0000313|EMBL:BBH17163.1, ECO:0000313|Proteomes:UP000271573};
RN [1] {ECO:0000313|EMBL:BBH17163.1, ECO:0000313|Proteomes:UP000271573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 39748 {ECO:0000313|EMBL:BBH17163.1,
RC ECO:0000313|Proteomes:UP000271573};
RA Kang S.W., Lee K.C., Kim K.K., Kim J.S., Kim D.S., Ko S.H., Yang S.H.,
RA Shin Y.K., Lee J.S.;
RT "Complete genome sequence of Nocardioides baekrokdamisoli strain KCTC
RT 39748.";
RL Submitted (NOV-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; AP019307; BBH17163.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G9IXN5; -.
DR KEGG; nbe:Back2_14500; -.
DR OrthoDB; 9768666at2; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000271573; 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; 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:UP000271573};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 7..287
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 320..387
FT /note="NADH-rubredoxin oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18267"
FT DOMAIN 419..467
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
FT DOMAIN 556..617
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 628..767
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
SQ SEQUENCE 846 AA; 90652 MW; 35592E10CCF289FC CRC64;
MSSYRKRIVV IGHGMVGHRF VEAAIERGLT ETYDIVILGE EPRAAYDRVA LTSYYEVGDK
ALSFLPSGKY ADPRVSLELN AKAVAVSPRA RIITLEDGRQ VEYDELVLAT GAYPFVPPVA
GKDLENVFVY RTIEDLIAIK KAAKKAKTGV VIGGGLLGLE AANAVKQLGL ETHVVELAPR
LMAVQIDSGA GKTLSREIEN LGLTVHTGAM TEAILGTKGK VSGLALKDRA TLNADIVVFS
AGIRPQDALG RAADLEIAER GGILVDEHCR TSEEHIWAIG ECAAPNGKMY GLVAPGYQMA
EVVVDSMLGG EGTFEGADMS TKLKLLGVDV ASFGDAHAET PGSLELVYSD AVAGIYKKLV
ISEDGKRLLG GVLVGDASAY GILRPMVASG LPLPDNPEDL ILPAGSGGLS KMELPDEAVV
CSCNNVTKGQ IKGAADNGCT TQADVTKETK AGSTCGSCKV QVKKIIEDHF AAQGVVVDKS
LCEHFPMTRA ELFDVVLVHG YRSFNEIIEA HGKGRGCDIC KPAVASILAS QLNSHVLDQG
NRQLQDTNDA YLGNLQKNGT YSVVPRIAGG EITPEGLIAI GEVAKDFGLY TKITGGQRID
LFGARLEQLP AVWKRLVDAG FESGHAYGKS LRTVKSCVGS TWCRYGQQDS VAMAIELELR
YRGLRSPHKL KGGVSGCARE CAEARGKDFG IIATTNGWNL YVGGNGGAIP AHAQLLAEDL
SDEDLRKYLD RFLMFYIRTA DRLQRTSTWL DSLEGGMDYL RQVVIEDSLG IAEELERAMA
SHIDSYFDEW KATIEDPEKV RRFMSFVNAP ETPDPNISFG TTRGQIVPEE SAGPVSLGMP
QIGASL
//
