ID A0A172YER3_9GAMM Unreviewed; 580 AA.
AC A0A172YER3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Sulfite reductase [NADPH] hemoprotein beta-component {ECO:0000256|HAMAP-Rule:MF_01540};
DE Short=SiR-HP {ECO:0000256|HAMAP-Rule:MF_01540};
DE Short=SiRHP {ECO:0000256|HAMAP-Rule:MF_01540};
DE EC=1.8.1.2 {ECO:0000256|HAMAP-Rule:MF_01540};
GN Name=cysI {ECO:0000256|HAMAP-Rule:MF_01540};
GN ORFNames=A5892_09955 {ECO:0000313|EMBL:ANF57748.1};
OS Halotalea alkalilenta.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halotalea.
OX NCBI_TaxID=376489 {ECO:0000313|EMBL:ANF57748.1, ECO:0000313|Proteomes:UP000077875};
RN [1] {ECO:0000313|EMBL:ANF57748.1, ECO:0000313|Proteomes:UP000077875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IHB B 13600 {ECO:0000313|EMBL:ANF57748.1,
RC ECO:0000313|Proteomes:UP000077875};
RA Swarnkar M.K., Sharma A., Kaushal K., Soni R., Rana S., Singh A.K.,
RA Gulati A.;
RT "Complete Genome Sequence of Halotalea alkalilenta IHB B 13600.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC Rule:MF_01540};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01540};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01540};
CC -!- COFACTOR:
CC Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01540};
CC Note=Binds 1 siroheme per subunit. {ECO:0000256|HAMAP-Rule:MF_01540};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen
CC sulfide from sulfite (NADPH route): step 1/1. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01540}.
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000256|ARBA:ARBA00010429, ECO:0000256|HAMAP-
CC Rule:MF_01540}.
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; CP015243; ANF57748.1; -; Genomic_DNA.
DR RefSeq; WP_064122675.1; NZ_CP015243.1.
DR AlphaFoldDB; A0A172YER3; -.
DR STRING; 376489.A5892_09955; -.
DR KEGG; haa:A5892_09955; -.
DR UniPathway; UPA00140; UER00207.
DR Proteomes; UP000077875; 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; Sulfite Reductase Hemoprotein, domain 1; 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 NCBIfam; TIGR02041; CysI; 1.
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; 1.
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, ECO:0000256|HAMAP-Rule:MF_01540};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01540};
KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192, ECO:0000256|HAMAP-
KW Rule:MF_01540};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|HAMAP-Rule:MF_01540};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01540};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01540};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01540};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01540};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01540}; Reference proteome {ECO:0000313|Proteomes:UP000077875}.
FT DOMAIN 80..137
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 176..331
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT DOMAIN 354..426
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT BINDING 444
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01540"
FT BINDING 450
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01540"
FT BINDING 489
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01540"
FT BINDING 493
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01540"
FT BINDING 493
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:0000256|HAMAP-Rule:MF_01540"
SQ SEQUENCE 580 AA; 65047 MW; D5A16C25A38A0A33 CRC64;
MTDIIAKLRD EDLTTYAANE KLKVDSDYLR GQLMEDMADI ATGAVSDGDL QLTKFHGFYL
QDDRDLRSER RQQKLEPLYS FMVRLRIPGG RLSTAQWLVM DRVATDYAND TLRVTTRQTL
QYHGVFKRNL RAHLKTINDV MVDTIAACGD VNRNVTSTAN PHRSRLHLEL FKLAAKISDH
LLPHTRAYHE IFLGEERVYG GPDEVVEPLY TKHYLPRKFK IGLALPPDNE IDIHTNDIGF
IAIVEGGEIV GFNVTVGGGM GSTHGEPDTY PRISDVIGYV PVDKAVDVAE KIMLVQRDNG
NRKSRKHARV KYTVDTMGIE GFKAELENYL GYALEPTRDH RFETTGDLLG WYQGEDGLWH
YGLFVENGRI KDYPEDSPIH AGMKLKSGLK AIAESFDGDI VMSCNQNVII SNVPEAAKAG
IDELLDKFNM VKSVTPLRQH SIACVALPTC GLAMAESERY LPTLLDKLDA VMRDAGLEQD
PIVLRMTGCP NGCGRPFMAE IGFVGKAIGR YNLYLGGNFT GTRLNKMYRE NIDEKTILEE
LTPMIHRYGR EREPGECFGD FVIRAGIIKA TVNGLDFHAQ
//
