ID A0A0J8R9Y2_COCIT Unreviewed; 304 AA.
AC A0A0J8R9Y2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Phosphoadenosine phosphosulfate reductase {ECO:0000313|EMBL:KMU80618.1};
GN ORFNames=CISG_08607 {ECO:0000313|EMBL:KMU80618.1};
OS Coccidioides immitis RMSCC 3703.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=454286 {ECO:0000313|EMBL:KMU80618.1, ECO:0000313|Proteomes:UP000054559};
RN [1] {ECO:0000313|Proteomes:UP000054559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 3703 {ECO:0000313|Proteomes:UP000054559};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate. {ECO:0000256|ARBA:ARBA00024327}.
CC -!- SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily.
CC {ECO:0000256|ARBA:ARBA00009732}.
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DR EMBL; DS268188; KMU80618.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8R9Y2; -.
DR STRING; 454286.A0A0J8R9Y2; -.
DR Proteomes; UP000054559; Unassembled WGS sequence.
DR GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; IEA:UniProtKB-EC.
DR GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IEA:InterPro.
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; IPR011800; PAPS_reductase_CysH.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00434; cysH; 1.
DR NCBIfam; TIGR02057; PAPS_reductase; 1.
DR PANTHER; PTHR46509; PHOSPHOADENOSINE PHOSPHOSULFATE REDUCTASE; 1.
DR PANTHER; PTHR46509:SF1; PHOSPHOADENOSINE PHOSPHOSULFATE REDUCTASE; 1.
DR Pfam; PF01507; PAPS_reduct; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054559}.
FT DOMAIN 72..249
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
FT REGION 245..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 304 AA; 34591 MW; 48AB909C71C36B40 CRC64;
MPASVHSTYP SDTDTCDIKE AESGYVSGDS SQPSLPDLVF TKPHLKFLNR QLQFLEPQDV
LRWCITSLPG LYQTTAFGLT GLVTIDMLSK LDVPRPQVVD LIFLDTLYHF PETLALVERV
RKRYPSLSIH VYKPQGAETA DEFAAKYGDR LWETNDQLYD WLAKVEPAQR AYRELQVSAV
LTGRRRSQGG KRGDLNIVEV DEAGLIKINP FANWGFQQVK DYITTHNVPY NELLDRGYKS
VGDWHSTQPV KEGEDERAGR WKGQAKTECG IHNPRSKYAQ FLREQEMKRQ QEALDQALQG
ADKA
//
