ID   A0A6N7LMR2_SINTE        Unreviewed;       557 AA.
AC   A0A6N7LMR2;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 1.
DT   28-JAN-2026, entry version 23.
DE   SubName: Full=Nitrite/sulfite reductase {ECO:0000313|EMBL:MQX18570.1};
GN   ORFNames=GHK62_28705 {ECO:0000313|EMBL:MQX18570.1};
OS   Sinorhizobium terangae.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=110322 {ECO:0000313|EMBL:MQX18570.1, ECO:0000313|Proteomes:UP000439983};
RN   [1] {ECO:0000313|EMBL:MQX18570.1, ECO:0000313|Proteomes:UP000439983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USDA4894 {ECO:0000313|EMBL:MQX18570.1,
RC   ECO:0000313|Proteomes:UP000439983};
RX   PubMed=23425606;
RA   Sugawara M., Epstein B., Badgley B.D., Unno T., Xu L., Reese J.,
RA   Gyaneshwar P., Denny R., Mudge J., Bharti A.K., Farmer A.D., May G.D.,
RA   Woodward J.E., Medigue C., Vallenet D., Lajus A., Rouy Z., Martinez-Vaz B.,
RA   Tiffin P., Young N.D., Sadowsky M.J.;
RT   "Comparative genomics of the core and accessory genomes of 48 Sinorhizobium
RT   strains comprising five genospecies.";
RL   Genome Biol. 14:0-R17(2013).
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:MQX18570.1}.
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DR   EMBL; WITC01000121; MQX18570.1; -; Genomic_DNA.
DR   RefSeq; WP_153442341.1; NZ_JACIGA010000011.1.
DR   AlphaFoldDB; A0A6N7LMR2; -.
DR   OrthoDB; 9803707at2; -.
DR   Proteomes; UP000439983; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.480.20; -; 2.
DR   Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 2.
DR   InterPro; IPR051329; NIR_SIR_4Fe-4S.
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   PANTHER; PTHR32439:SF9; BLR3264 PROTEIN; 1.
DR   PANTHER; PTHR32439; FERREDOXIN--NITRITE REDUCTASE, CHLOROPLASTIC; 1.
DR   Pfam; PF01077; NIR_SIR; 2.
DR   Pfam; PF03460; NIR_SIR_ferr; 2.
DR   SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 2.
DR   SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 2.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000439983}.
FT   DOMAIN          52..110
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          119..273
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
FT   DOMAIN          330..398
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          410..529
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
SQ   SEQUENCE   557 AA;  62024 MW;  5738BC77728CCB62 CRC64;
     MYRYDEFDHA FVSARVEQFR DQVQRRLSGE LAEDAFKPLR LMNGVYLQLH AYMLRVAIPY
     GTLSSRQMRM LAHIARKYDR GYGHFTTRQN IQYNWPRLSD TPDILNELAS VEMHALQTSG
     NCIRNVTADH FSGAAADEIA DPRPYAEILR QWSSVHPEFS FLPRKFKIAV TGAERDRAAI
     QVHDIGLHLK KDENGRLGFA VYVGGGQGRT PLIAKKIRDF LPEEDLLSYT TAIMRVYNLY
     GRRDNKYKAR IKILVHETGA EELARQVEVE FAKLKDTELK LPDADIQAIS AYFAPATLPN
     RAEGWGNLAR WKKADPEFAR WVQQNVQPHK HPDYGMVTIS LKPIGGIPGD ASDAQMDAVA
     DIAEEYAFDE IRVSHEQNLI LPHVALADLE PVYRALVAAG LATANAGLIT DIIACPGLDY
     CALANARSIP VAQEISNRFG SPERQAEIGE LKIKISGCIN ACGHHHVGHI GLLGVEKKGA
     ELYQITLGGS GDENTSIGEI IGRGFEPEKV TDAVETIVDT YLGLRRDKTE TFLEAYRRVG
     PQPFKDALYG GSAQEAA
//