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Database: UniProt
Entry: A0A231HNS0_9BURK
LinkDB: A0A231HNS0_9BURK
Original site: A0A231HNS0_9BURK 
ID   A0A231HNS0_9BURK        Unreviewed;       579 AA.
AC   A0A231HNS0;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Sulfite reductase {ECO:0000313|EMBL:OXR50518.1};
GN   ORFNames=PuT2_01205 {ECO:0000313|EMBL:OXR50518.1};
OS   Pusillimonas sp. T2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Pusillimonas.
OX   NCBI_TaxID=1548123 {ECO:0000313|EMBL:OXR50518.1, ECO:0000313|Proteomes:UP000216496};
RN   [1] {ECO:0000313|EMBL:OXR50518.1, ECO:0000313|Proteomes:UP000216496}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T2 {ECO:0000313|EMBL:OXR50518.1,
RC   ECO:0000313|Proteomes:UP000216496};
RA   Yuan M., Qiu J.G., Ma Y.;
RT   "The genome sequence of Pusillimonas sp. T2.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC         Evidence={ECO:0000256|ARBA:ARBA00001929};
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:OXR50518.1}.
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DR   EMBL; NIQA01000001; OXR50518.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A231HNS0; -.
DR   OrthoDB; 3189055at2; -.
DR   Proteomes; UP000216496; 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:InterPro.
DR   Gene3D; 3.90.480.20; -; 1.
DR   Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 2.
DR   Gene3D; 3.90.480.10; Sulfite Reductase Hemoprotein;Domain 2; 1.
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; IPR045169; NO2/SO3_Rdtase_4Fe4S_prot.
DR   InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR   PANTHER; PTHR11493:SF47; SULFITE REDUCTASE [NADPH] SUBUNIT BETA; 1.
DR   PANTHER; PTHR11493; SULFITE REDUCTASE [NADPH] SUBUNIT BETA-RELATED; 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   Reference proteome {ECO:0000313|Proteomes:UP000216496}.
FT   DOMAIN          53..109
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          119..271
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
FT   DOMAIN          346..398
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          410..557
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
SQ   SEQUENCE   579 AA;  64178 MW;  9F7023D15A1EFD06 CRC64;
     MYTYNETDQQ LVNERVAQFE GQTQRFLAGE LTEDEFRTLR LQNGLYIQRH APMLRVAIPY
     GLLRADQLRK LADIARRYDR GYGHFSTRQN MQFNWPRLED VPAILGELAT VQLHAIQTSG
     NCIRNTTSDH LAGVAPDEIV NPLVWCEIIR QWSTFHPEFA FLPRKFKIAV SGATTDRAAI
     AVNDIGLQAV TQNGETGFQV WAGGGLGRTP IVGKQISPFV PWPHLLTYLS AILRVYNLHG
     RRDNKYKARI KILVRDMTPE GFAKAVDEHW QALKNGPDTL TQAHVDQIAS RFNWPVYQAF
     EAGHDSQVTE LKANNPAFAR WLRTNTHAHK VAGYAAVSVS LKPTGSPPGD ITADQMDSIA
     TLAEQYSQGQ LRVTHEQNLL LPAVPRQDLP ALWHALNALG LATPNIGLLT NIISCPGGDF
     CALANAVSIP VAAAIQARFD DLDYLHDIGE LDLNISGCIN ACGHHHVGHI GILGVDKAGQ
     EWYQVTLGGR QSAARTEQVG DTGAEIGRII GPSFSREQIP DVIERLIQTY LGLRDDDTER
     FIDVIDRVGP EPFKTAVYSD PNIVTGKIQH TRNEEDAHA
//
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