CYSH_MYCS2
ID CYSH_MYCS2 Reviewed; 236 AA.
AC A0R0W2; I7GDN9;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Adenosine 5'-phosphosulfate reductase {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000303|PubMed:12072441};
DE Short=APS reductase {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000303|PubMed:12072441};
DE EC=1.8.4.10 {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000269|PubMed:12072441};
DE AltName: Full=5'-adenylylsulfate reductase {ECO:0000255|HAMAP-Rule:MF_00063};
DE AltName: Full=Thioredoxin-dependent 5'-adenylylsulfate reductase {ECO:0000255|HAMAP-Rule:MF_00063};
GN Name=cysH {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000303|PubMed:12072441};
GN OrderedLocusNames=MSMEG_4528 {ECO:0000312|EMBL:ABK74710.1},
GN MSMEI_4415 {ECO:0000312|EMBL:AFP40869.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=12072441; DOI=10.1074/jbc.m204613200;
RA Williams S.J., Senaratne R.H., Mougous J.D., Riley L.W., Bertozzi C.R.;
RT "5'-adenosinephosphosulfate lies at a metabolic branch point in
RT mycobacteria.";
RL J. Biol. Chem. 277:32606-32615(2002).
CC -!- FUNCTION: Catalyzes the formation of sulfite from adenosine 5'-
CC phosphosulfate (APS) using thioredoxin as an electron donor.
CC {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000269|PubMed:12072441}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + AMP + 2 H(+) + sulfite =
CC [thioredoxin]-dithiol + adenosine 5'-phosphosulfate;
CC Xref=Rhea:RHEA:21976, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:50058, ChEBI:CHEBI:58243, ChEBI:CHEBI:456215;
CC EC=1.8.4.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00063,
CC ECO:0000269|PubMed:12072441};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00063};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00063};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate. {ECO:0000255|HAMAP-Rule:MF_00063,
CC ECO:0000305|PubMed:12072441}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00063}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene confers cysteine and
CC methionine auxotrophy. {ECO:0000269|PubMed:12072441}.
CC -!- SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00063}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFP40869.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK74710.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP40869.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011729897.1; NZ_SIJM01000052.1.
DR RefSeq; YP_888800.1; NC_008596.1.
DR AlphaFoldDB; A0R0W2; -.
DR SMR; A0R0W2; -.
DR STRING; 246196.MSMEI_4415; -.
DR EnsemblBacteria; ABK74710; ABK74710; MSMEG_4528.
DR EnsemblBacteria; AFP40869; AFP40869; MSMEI_4415.
DR GeneID; 66735855; -.
DR KEGG; msg:MSMEI_4415; -.
DR KEGG; msm:MSMEG_4528; -.
DR PATRIC; fig|246196.19.peg.4430; -.
DR eggNOG; COG0175; Bacteria.
DR OMA; PIARWTQ; -.
DR OrthoDB; 674332at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043866; F:adenylyl-sulfate reductase (thioredoxin) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:InterPro.
DR GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IEA:UniProtKB-UniRule.
DR CDD; cd01713; PAPS_reductase; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00063; CysH; 1.
DR InterPro; IPR011798; APS_reductase.
DR InterPro; IPR004511; PAPS/APS_Rdtase.
DR InterPro; IPR002500; PAPS_reduct.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01507; PAPS_reduct; 1.
DR PIRSF; PIRSF000857; PAPS_reductase; 1.
DR TIGRFAMs; TIGR02055; APS_reductase; 1.
DR TIGRFAMs; TIGR00434; cysH; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..236
FT /note="Adenosine 5'-phosphosulfate reductase"
FT /id="PRO_0000452768"
FT ACT_SITE 231
FT /note="Nucleophile; cysteine thiosulfonate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
FT BINDING 122
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
FT BINDING 123
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
FT BINDING 205
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
FT BINDING 208
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
SQ SEQUENCE 236 AA; 25692 MW; 27267B9EF0E96746 CRC64;
MTDVTTSTEN ELRELAERGA AELADASAEE LLRWTDEHFG GNYVVASNMQ DAVLVEMAAK
VRPGVDVLFL DTGYHFAETI GTRDAVEAVY DVHVVNVTPE RTVAEQDELL GKNLFARDPG
ECCRLRKVVP LTNALKGYSA WVTGIRRVEA PTRANAPLIS WDNAFGLVKI NPIAAWTDED
MQNYIDANGI LVNPLVYEGY PSIGCAPCTS KPIPGADPRS GRWAGLSKTE CGLHVS
