ID A0A0F6QXK6_9CORY Unreviewed; 260 AA.
AC A0A0F6QXK6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Phosphoadenosine 5'-phosphosulfate reductase {ECO:0000256|HAMAP-Rule:MF_00063};
DE Short=PAPS reductase {ECO:0000256|HAMAP-Rule:MF_00063};
DE EC=1.8.4.8 {ECO:0000256|HAMAP-Rule:MF_00063};
DE AltName: Full=3'-phosphoadenylylsulfate reductase {ECO:0000256|HAMAP-Rule:MF_00063};
DE AltName: Full=PAPS reductase, thioredoxin dependent {ECO:0000256|HAMAP-Rule:MF_00063};
DE AltName: Full=PAPS sulfotransferase {ECO:0000256|HAMAP-Rule:MF_00063};
DE AltName: Full=PAdoPS reductase {ECO:0000256|HAMAP-Rule:MF_00063};
GN Name=cysH {ECO:0000256|HAMAP-Rule:MF_00063,
GN ECO:0000313|EMBL:AKE40037.1};
GN ORFNames=NG00_01883 {ECO:0000313|EMBL:AVH89121.1}, UL81_10515
GN {ECO:0000313|EMBL:AKE40037.1};
OS Corynebacterium camporealensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=161896 {ECO:0000313|EMBL:AKE40037.1, ECO:0000313|Proteomes:UP000033566};
RN [1] {ECO:0000313|EMBL:AVH89121.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 105508 {ECO:0000313|EMBL:AVH89121.1};
RA Seo M.-J., Seok Y.J., Cha I.-T.;
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000029996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 105508 {ECO:0000313|Proteomes:UP000029996};
RA Hassan S.S., Tiwari S., Jamal S.B., Oliveira L.D.C., Souza F.,
RA Mariano D.C., Almeida S., Dorella F., Pereira F., Carvalho A., Leal C.A.,
RA Soares S.D.C., Figueiredo H.C., Silva A., Azevedo V.A.;
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AKE40037.1, ECO:0000313|Proteomes:UP000033566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44610 {ECO:0000313|EMBL:AKE40037.1,
RC ECO:0000313|Proteomes:UP000033566};
RX PubMed=26021938;
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete Genome Sequence of Corynebacterium camporealensis DSM 44610,
RT Isolated from the Milk of a Manchega Sheep with Subclinical Mastitis.";
RL Genome Announc. 3:e00572-15(2015).
RN [4] {ECO:0000313|EMBL:AVH89121.1, ECO:0000313|Proteomes:UP000029996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 105508 {ECO:0000313|EMBL:AVH89121.1,
RC ECO:0000313|Proteomes:UP000029996};
RA Coimbra N., Jamal S.B., Jaiswal A., Silva A.L., Azevedo V.;
RT "Genome sequencing of Corynebacterium camporealensis CIP 105508.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of sulfite from phosphoadenosine 5'-
CC phosphosulfate (PAPS) using thioredoxin as an electron donor.
CC {ECO:0000256|HAMAP-Rule:MF_00063}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + adenosine 3',5'-bisphosphate + 2
CC H(+) + sulfite = 3'-phosphoadenylyl sulfate + [thioredoxin]-dithiol;
CC Xref=Rhea:RHEA:11724, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:50058, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343; EC=1.8.4.8;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00063};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 3/3. {ECO:0000256|HAMAP-Rule:MF_00063}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00063}.
CC -!- SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily.
CC {ECO:0000256|ARBA:ARBA00009732, ECO:0000256|HAMAP-Rule:MF_00063}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00063}.
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DR EMBL; CP011311; AKE40037.1; -; Genomic_DNA.
DR EMBL; CP027001; AVH89121.1; -; Genomic_DNA.
DR RefSeq; WP_046453569.1; NZ_CP027001.1.
DR AlphaFoldDB; A0A0F6QXK6; -.
DR STRING; 161896.UL81_10515; -.
DR KEGG; ccj:UL81_10515; -.
DR PATRIC; fig|161896.4.peg.2051; -.
DR HOGENOM; CLU_044089_2_0_11; -.
DR OrthoDB; 9794018at2; -.
DR UniPathway; UPA00140; UER00206.
DR Proteomes; UP000029996; Chromosome.
DR Proteomes; UP000033566; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
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; HUPs; 1.
DR HAMAP; MF_00063; CysH; 1.
DR InterPro; IPR004511; PAPS/APS_Rdtase.
DR InterPro; IPR002500; PAPS_reduct.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00434; cysH; 1.
DR PANTHER; PTHR46509; PHOSPHOADENOSINE PHOSPHOSULFATE REDUCTASE; 1.
DR PANTHER; PTHR46509:SF1; PHOSPHOADENOSINE PHOSPHOSULFATE REDUCTASE; 1.
DR Pfam; PF01507; PAPS_reduct; 1.
DR PIRSF; PIRSF000857; PAPS_reductase; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00063};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00063}; Reference proteome {ECO:0000313|Proteomes:UP000033566}.
FT DOMAIN 70..234
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 256
FT /note="Nucleophile; cysteine thiosulfonate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
SQ SEQUENCE 260 AA; 28952 MW; B15729A25786B4EC CRC64;
MTSHIDLVSG GEYRDPAQSP EGTRDTAELP AGIAKRNREL VEQWAEKLHD ASAEEICAWA
AEYAPGRLAV TMSMENTVLA ELAQGAGLDA DLLFIDTGWH FPETLETADK VEERYPDLSL
VRVKPLLSPE EQDRIYGPRL YARDVAAYNR MRKVEPLNMA MDDYCGWVTG LRRADSEHRA
DAPALSLDRT GRLKISPIIT WDLEDTDRYI ADHDLIIHPL TLQGYRSIGC APLTFPVGEG
EDARSGRVFA DGKTECGLHE
//
