ID U5WS52_MYCKA Unreviewed; 857 AA.
AC U5WS52;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=assimilatory sulfite reductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012353};
DE EC=1.8.7.1 {ECO:0000256|ARBA:ARBA00012353};
GN ORFNames=MKAN_16830 {ECO:0000313|EMBL:AGZ51757.1};
OS Mycobacterium kansasii ATCC 12478.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=557599 {ECO:0000313|EMBL:AGZ51757.1, ECO:0000313|Proteomes:UP000017786};
RN [1] {ECO:0000313|EMBL:AGZ51757.1, ECO:0000313|Proteomes:UP000017786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12478 {ECO:0000313|EMBL:AGZ51757.1,
RC ECO:0000313|Proteomes:UP000017786};
RG McGill University Mycobacterium genome consortium;
RA Veyrier F.J., Behr M.A.;
RT "Genome sequence of Mycobacterium kansasii.";
RL Submitted (OCT-2013) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP006835; AGZ51757.1; -; Genomic_DNA.
DR AlphaFoldDB; U5WS52; -.
DR KEGG; mkn:MKAN_16830; -.
DR eggNOG; COG1251; Bacteria.
DR HOGENOM; CLU_003291_0_0_11; -.
DR OrthoDB; 9768666at2; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000017786; 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; 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; 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; 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 Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 19..306
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 343..403
FT /note="NADH-rubredoxin oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18267"
FT DOMAIN 445..492
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
FT DOMAIN 577..638
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 649..786
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
SQ SEQUENCE 857 AA; 91008 MW; 07D85056ABFBDCBC CRC64;
MASAGTTRAR DGESPCRRHV IVVGHGMVGH RLVEALRARD TSGLWRITVL AEEGDAAYDR
VGLTSYTETW DRGQLALPGN DYAGDDRVRL LLNTRVTEID RATKSVVTAD GQRHSYDALV
LATGSYAFVP PVPGHDLPEC HVYRTLDDLD AIRAGAQHTL NSAHTDAGVV IGGGLLGLEA
ANALRQFGLQ PHVVEMMPRL MAQQIDEAGG ALLARMITDL GIAVHVGTGT ESIEPVEHSD
GSATVRVRLT DGDTIDAGVV IFAAGIRPRD ELPKAAGLAI AERGGVLTDL SCRTSDPDIY
AVGEVAAIEG CCYGLVGPGY TSAEVVADRL LGGAAEFPEA DLSTKLKLLG VDVASFGDAM
GATENCLEVV INDAVKRTYA KLVLSDDAKT LLGGVLVGDA SSYGVLRPMV GSELPGDPLA
LIAPAGSGPG GGGLGVGALP DSAQICSCNN VTKGDLKCAI ADGCADVPAL KACTAAGTSC
GSCVPLLKQL LEAEGVEQSK ALCEHFSQSR AELFEIISAT EIRTFSGLLE RFGRGKGCDI
CKPVVASILA STGSDHILDG EQAALQDSND HFLANIQKNG SYSVVPRVPG GDIKPEHLIL
IGQIAQEFGL YTKITGGQRI DMFGARVDQL PLIWKRLVDA GMESGHAYGK ALRTVKSCVG
SDWCRYGQQD SVQLAIDLEL RYRGLRAPHK IKLGVSGCAR ECAEARGKDV GVIATEKGWN
LYVGGNGGMT PKHAQLLAGD LDTETLVRYI DRFLMYYIRT ADRLQRTAPW VESLGLDHVR
EVVCEDSLGL AEEFEAAMER HVANYKCEWK GVLEDPDKLS RFVSFVNAPD AVDSTVTFTE
RAGRKVPVPI GMPRMRS
//
