GenomeNet

Database: UniProt
Entry: A0A1E7JIA7_9ACTN
LinkDB: A0A1E7JIA7_9ACTN
Original site: A0A1E7JIA7_9ACTN 
ID   A0A1E7JIA7_9ACTN        Unreviewed;       565 AA.
AC   A0A1E7JIA7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, 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=AN215_28255 {ECO:0000313|EMBL:OEU86187.1};
OS   Streptomyces abyssalis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=933944 {ECO:0000313|EMBL:OEU86187.1, ECO:0000313|Proteomes:UP000176087};
RN   [1] {ECO:0000313|EMBL:OEU86187.1, ECO:0000313|Proteomes:UP000176087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCSIO 10390 {ECO:0000313|EMBL:OEU86187.1,
RC   ECO:0000313|Proteomes:UP000176087};
RX   PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA   Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA   Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT   "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT   Adaptation to the Marine Environment and Their Diversity at the Genomic
RT   Level.";
RL   Front. Microbiol. 7:998-998(2016).
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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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:OEU86187.1}.
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; LJGT01000041; OEU86187.1; -; Genomic_DNA.
DR   RefSeq; WP_070010403.1; NZ_LJGT01000041.1.
DR   AlphaFoldDB; A0A1E7JIA7; -.
DR   STRING; 933944.AN215_28255; -.
DR   PATRIC; fig|933944.5.peg.3604; -.
DR   OrthoDB; 3189055at2; -.
DR   Proteomes; UP000176087; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0050311; F:sulfite reductase (ferredoxin) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.90.480.20; -; 1.
DR   Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 2.
DR   InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
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   PANTHER; PTHR32439; FERREDOXIN--NITRITE REDUCTASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR32439:SF0; FERREDOXIN--NITRITE REDUCTASE, CHLOROPLASTIC; 1.
DR   Pfam; PF01077; NIR_SIR; 2.
DR   Pfam; PF03460; NIR_SIR_ferr; 2.
DR   PRINTS; PR00397; SIROHAEM.
DR   SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 2.
DR   SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 2.
DR   PROSITE; PS00365; NIR_SIR; 1.
PE   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00022617};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022617};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000176087};
KW   Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT   DOMAIN          101..162
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          172..323
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
FT   DOMAIN          349..414
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          426..558
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   565 AA;  62434 MW;  3F9B77692667CDAE CRC64;
     MADTSKRPAS APSRRKAGRH RGEGQWAAGH FTPLNGNEQT KKDDDGLNVR TRIETIYAHR
     GFDSIDGADL RGRMRWWGLY TQRRPGISGG KTAVLEPEEL DDEYFMLRVR IDGGQLTTQQ
     LRTVGEISQD FARGTADITD RQNIQFHWIR IEDMPEIWRR LEGVGLSTTE ACGDTPRVIM
     GSPVAGIAAD EIIDGTPAID EIHRRVIGNP AYSNLPRKFK TAVSGSPLLD VAHEINDVAF
     VGVEHPELGP GFDVWVGGGL STNPKLGVRL GAWVPIEDVA DVHEGIVSVF RDYGYRRLRT
     RARIKFLVAD WGAEKFRQVL EDEYLLRRMA DGPAPEAPVQ QWRDHIGVHE QRDGNHYVGF
     APRVGRIDGG TLAKIADLAE SHGSGRVRTT AEQKMIVLDV AGDQVESLTE GLEALDLTAR
     PSVFRRGTMA CTGIEFCKLA IVETKARGSS LIDELEQRLP HFDEPVTINL NGCPNSCARI
     QVADIGLKGQ LVTDADGEQV EGYQVHLGGS LGMEPGFGRK VRGLKVTAAE LPDYIERVLL
     NFKEQREDGE RFAQWAARAE EGALK
//
DBGET integrated database retrieval system