ID A0A917V768_9NOCA Unreviewed; 845 AA.
AC A0A917V768;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 16.
DE RecName: Full=assimilatory sulfite reductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012353};
DE EC=1.8.7.1 {ECO:0000256|ARBA:ARBA00012353};
GN ORFNames=GCM10011591_16570 {ECO:0000313|EMBL:GGK45778.1};
OS Nocardia camponoti.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Nocardiaceae; Nocardia.
OX NCBI_TaxID=1616106 {ECO:0000313|EMBL:GGK45778.1, ECO:0000313|Proteomes:UP000612956};
RN [1] {ECO:0000313|EMBL:GGK45778.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 4.7278 {ECO:0000313|EMBL:GGK45778.1};
RX PubMed=25193709;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Walter F., Albersmeier A., Kalinowski J., Ruckert C.;
RT "Complete genome sequence of Corynebacterium casei LMG S-19264T (=DSM
RT 44701T), isolated from a smear-ripened cheese.";
RL Int. J. Syst. Evol. Microbiol. 189:76-77(2014).
RN [2] {ECO:0000313|EMBL:GGK45778.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CGMCC 4.7278 {ECO:0000313|EMBL:GGK45778.1};
RA Sun Q., Zhou Y.;
RL Submitted (SEP-2020) 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=hydrogen sulfide + 6 oxidized [2Fe-2S]-[ferredoxin] + 3 H2O =
CC sulfite + 6 reduced [2Fe-2S]-[ferredoxin] + 7 H(+);
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:ARBA00049518};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRNR:PIRNR037149};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|PIRSR:PIRSR037149-1};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000256|PIRSR:PIRSR037149-1};
CC -!- COFACTOR:
CC Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC Evidence={ECO:0000256|PIRSR:PIRSR037149-1};
CC Note=Binds 1 siroheme per subunit. {ECO:0000256|PIRSR:PIRSR037149-1};
CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC {ECO:0000256|ARBA:ARBA00005096}.
CC -!- SUBUNIT: Homodimer which associates with NirD.
CC {ECO:0000256|ARBA:ARBA00064211}.
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:GGK45778.1}.
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DR EMBL; BMMW01000002; GGK45778.1; -; Genomic_DNA.
DR RefSeq; WP_188828342.1; NZ_BMMW01000002.1.
DR AlphaFoldDB; A0A917V768; -.
DR Proteomes; UP000612956; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0098809; F:nitrite reductase activity; IEA:InterPro.
DR GO; GO:0050311; F:sulfite reductase (ferredoxin) activity; IEA:UniProtKB-EC.
DR GO; GO:0015980; P:energy derivation by oxidation of organic compounds; IEA:UniProtKB-ARBA.
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 FunFam; 3.30.413.10:FF:000007; Nitrite reductase [NAD(P)H] large subunit; 1.
DR FunFam; 3.50.50.60:FF:000033; Nitrite reductase [NAD(P)H], large subunit; 1.
DR FunFam; 1.10.10.1100:FF:000002; Nitrite reductase large subunit; 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; IPR052034; NasD-like.
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 NCBIfam; NF011565; PRK14989.1; 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 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRSR:PIRSR037149-1};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR037149};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR037149};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR037149-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR037149-1};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR037149-
KW 1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR037149-1};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063,
KW ECO:0000256|PIRNR:PIRNR037149};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000612956};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 7..290
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 424..471
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..749
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT BINDING 637
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR037149-1"
FT BINDING 643
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR037149-1"
FT BINDING 677
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR037149-1"
FT BINDING 681
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR037149-1"
FT BINDING 681
FT /ligand="siroheme"
FT /ligand_id="ChEBI:CHEBI:60052"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR037149-1"
SQ SEQUENCE 845 AA; 88753 MW; 3E3EC499A07663A3 CRC64;
MNTQRKTVVV VGHGMVGHRF VEALRSRDEA GQWQIIVLSE EALPAYDRVG LSYYVGNWNP
DDLALPGNTY EGDELVDLRL GQRGESIDLA AKTVTSTDGT VIAYDALVMA TGSYPFVPPV
PGHDLPECFV YRTIDDLDGI RAAAEAAGPG AHGVVVGGGL LGLEAANALR LLGMVPHVIE
YNNRLMPAQV DAGGGAILEK LVTDIGLNVH TGVGTAKIVS IDETGSDKVT IHLSDESEIK
ASLVVFSAGV RPQDALAKAS GLEIGARGGI LTDLALQTSD PSVYAIGECA AIEGVCYGLV
APGYTTAEIV ADRILGGEGT FPGADMSTKL KLMGVDVASF GDAHATSEGA LEVVLHDAAK
GTYAKLVVSD DAKTLLGGIL VGDASQYAAL RPLVGRPLPA DAAALISPAG AELGADALPD
DAQICSCNNV SKGAICGAIA DGACDIPAVK SCTNAGTSCG GCVPMIKKLL EQSGVALSKA
LCEHFGQSRA ELFDIIAVTG IRTFSELIAR YGKGTGCDIC KPTVASILAS TSSDHILEGE
QAALQDTNDH FLANLQKNGT YSVVPRMPGG EVTADQLIVI GEVAKEFGLY VKVTGGQRID
LFGARVEQLP LIWKRLVDVG MESGHAYGKS LRTVKSCVGS TWCRYGQQDS VGMAVLLEKR
YRGLRSPHKI KLAVSGCARE CAEARGKDVG VIATEHGWNL YVGGNGGLTP KHAVLLAGDL
DDETLIRYID RYLMFYVRTA DRLQRTAPWQ EALEGGIDYL KAVVCDDSLG IAADLEAAMD
RHVDGYKDEW AAVLEDENKL SRFVSFVNAP DEADSTISFD DSGDRKVPVL LGLPSVPVGT
AVSGK
//
