CYSI_PHOLL
ID CYSI_PHOLL Reviewed; 576 AA.
AC Q7N8L5;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Sulfite reductase [NADPH] hemoprotein beta-component {ECO:0000255|HAMAP-Rule:MF_01540};
DE Short=SiR-HP {ECO:0000255|HAMAP-Rule:MF_01540};
DE Short=SiRHP {ECO:0000255|HAMAP-Rule:MF_01540};
DE EC=1.8.1.2 {ECO:0000255|HAMAP-Rule:MF_01540};
GN Name=cysI {ECO:0000255|HAMAP-Rule:MF_01540}; OrderedLocusNames=plu0704;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
CC -!- FUNCTION: Component of the sulfite reductase complex that catalyzes the
CC 6-electron reduction of sulfite to sulfide. This is one of several
CC activities required for the biosynthesis of L-cysteine from sulfate.
CC {ECO:0000255|HAMAP-Rule:MF_01540}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH +
CC sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.8.1.2; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01540};
CC -!- COFACTOR:
CC Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01540};
CC Note=Binds 1 siroheme per subunit. {ECO:0000255|HAMAP-Rule:MF_01540};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01540};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01540};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen
CC sulfide from sulfite (NADPH route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01540}.
CC -!- SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein, the
CC beta component is a hemoprotein. {ECO:0000255|HAMAP-Rule:MF_01540}.
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000255|HAMAP-Rule:MF_01540}.
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DR EMBL; BX571861; CAE12999.1; -; Genomic_DNA.
DR RefSeq; WP_011145080.1; NC_005126.1.
DR AlphaFoldDB; Q7N8L5; -.
DR SMR; Q7N8L5; -.
DR STRING; 243265.plu0704; -.
DR EnsemblBacteria; CAE12999; CAE12999; plu0704.
DR GeneID; 24167941; -.
DR KEGG; plu:plu0704; -.
DR eggNOG; COG0155; Bacteria.
DR HOGENOM; CLU_001975_3_2_6; -.
DR OMA; MGMTHGD; -.
DR OrthoDB; 1588103at2; -.
DR BioCyc; PLUM243265:PLU_RS03515-MON; -.
DR UniPathway; UPA00140; UER00207.
DR Proteomes; UP000002514; Chromosome.
DR GO; GO:0009337; C:sulfite reductase complex (NADPH); IEA:InterPro.
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:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.413.10; -; 2.
DR HAMAP; MF_01540; CysI; 1.
DR InterPro; IPR011786; CysI.
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; PTHR11493; 1.
DR Pfam; PF01077; NIR_SIR; 2.
DR Pfam; PF03460; NIR_SIR_ferr; 2.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF55124; SSF55124; 2.
DR SUPFAM; SSF56014; SSF56014; 2.
DR TIGRFAMs; TIGR02041; CysI; 1.
DR PROSITE; PS00365; NIR_SIR; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Amino-acid biosynthesis; Cysteine biosynthesis; Heme; Iron;
KW Iron-sulfur; Metal-binding; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..576
FT /note="Sulfite reductase [NADPH] hemoprotein beta-
FT component"
FT /id="PRO_0000199903"
FT BINDING 435
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT BINDING 441
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT BINDING 480
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT BINDING 484
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01540"
FT BINDING 484
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:0000255|HAMAP-Rule:MF_01540"
SQ SEQUENCE 576 AA; 64829 MW; 3CA6B1166715B15D CRC64;
MNDKQHGPFI VEGKLADSER MKQESNFLRG TISEDLTNGL TGGFEGDNFL LIRFHGMYQQ
DDRDIRAERA EQKLEPRHAI MLRCRLPGGV ITPQQWLGID KFAEENTLYG SIRLTNRQTF
QFHGILKGKV KLAHQLLNQV GLDSLATAND VNRNVLCTSN PIQSELHQQA YEWAKKISEH
LLPRTRAYAE LWLDKEKVAT TDEEPILGST YLPRKFKTTV VIPPQNDVDL HANDLNFIAI
AEGSKLVGFN VLVGGGLAMT HGDKNTYPSM ASEFGYIPLE HTLAIAEAVV TTQRDWGNRT
ERKNAKTKYT LERVGVETFK AEVERRAGVK FEAIRPYEFT GRGDQIGWLK GIDDKWHLTL
FIENGRLLDY PGKPLKSGVA EIAKIHKGDF RLTANQNLII AGIPESEKQR IETIACRHGL
IDDKTTVQRK NSMACVSFPT CPLAMAEAER FLPEFVTHVE QLMNKHGIGD EHIVLRVTGC
PNGCARAMLA EVGLVGKALD RYNLHLGGNR IGTRIPRMYK ENISSQAILS IMDELIGRWA
TGRQPNEGFG DFLIRTDIIK PVLDSARDFY DWQEAV
