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Database: UniProt
Entry: Q04PC9_LEPBJ
LinkDB: Q04PC9_LEPBJ
Original site: Q04PC9_LEPBJ 
ID   Q04PC9_LEPBJ            Unreviewed;       560 AA.
AC   Q04PC9;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   SubName: Full=Sulfite reductase (NADPH), alpha subunit {ECO:0000313|EMBL:ABJ77241.1};
GN   Name=cysI {ECO:0000313|EMBL:ABJ77241.1};
GN   OrderedLocusNames=LBJ_2837 {ECO:0000313|EMBL:ABJ77241.1};
OS   Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=355277 {ECO:0000313|EMBL:ABJ77241.1, ECO:0000313|Proteomes:UP000000656};
RN   [1] {ECO:0000313|EMBL:ABJ77241.1, ECO:0000313|Proteomes:UP000000656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB197 {ECO:0000313|EMBL:ABJ77241.1,
RC   ECO:0000313|Proteomes:UP000000656};
RX   PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA   Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA   Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA   Rood J.I., Davies J.K., Adler B.;
RT   "Genome reduction in Leptospira borgpetersenii reflects limited
RT   transmission potential.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC       family. {ECO:0000256|ARBA:ARBA00010429}.
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DR   EMBL; CP000350; ABJ77241.1; -; Genomic_DNA.
DR   RefSeq; WP_011672097.1; NC_008510.1.
DR   AlphaFoldDB; Q04PC9; -.
DR   KEGG; lbj:LBJ_2837; -.
DR   HOGENOM; CLU_001975_3_2_12; -.
DR   Proteomes; UP000000656; Chromosome 1.
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; -; 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; IPR045169; NO2/SO3_Rdtase_4Fe4S_prot.
DR   InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR   InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
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   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   3: Inferred from homology;
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}.
FT   DOMAIN          65..130
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          164..321
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
FT   DOMAIN          342..408
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          462..557
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
SQ   SEQUENCE   560 AA;  62548 MW;  7958DE6C1FCB7905 CRC64;
     MSETKELSPV EEIKLNSRNL RGKIAEGLDR NIDSYEEDEK QLLKFHGLYQ QKDRDRKKDE
     SGNDMEAPTS FMIRGRIPGG RLTPEQYLVW DELGDKFGGG AIRLTTRQSV QLHTLRIFHL
     RDVMKAIHEV NLSSMGACGD VVRNVTQAVN PLGKKELQLL DGVSQILSDH FKYKTNAYAE
     VWLGDKQLNK DEEETIYGKT YLPRKFKIAV TLAGNNTVDI YANDMGFAAT LSANGKIDGY
     FVFAGGGFGM THNKPETFAR AASLLGWIPE SALIPVAEAI VTAHRDFGDR TNRKHARLKY
     VLAEKGVDWF RSEVESRSNV KLDTDKSLPS WKTPSYLGWN EREDGTLSLG FHTLAGRIKD
     FPGRPLKSAL REIIGIYKLH VQITADQDLI LIGIQKSDRE KIEKRLQELN VPWKSPSPLY
     DRALACPALP TCALALTESE RSFPEVLNGI QKVLDKLGLG DRALVVRMTG CPNGCARPYS
     AEVGIVGQQA GGKYSLFFGA DSEGTKVGEY VAKKVALADI PAQLEKVFVL WKEEGDSDEK
     FGDFVNRFPL ERFREVLGSM
//
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