MET16_EMENI
ID MET16_EMENI Reviewed; 306 AA.
AC P56859; C8VAQ1; Q5B3W0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 3.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Phosphoadenosine phosphosulfate reductase;
DE EC=1.8.4.8;
DE AltName: Full=3'-phosphoadenylylsulfate reductase;
DE AltName: Full=PAPS reductase, thioredoxin dependent;
DE AltName: Full=PAdoPS reductase;
GN Name=sA; ORFNames=AN4770;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7770049; DOI=10.1007/bf00293143;
RA Borges-Walmsley M.I., Turner G., Bailey A.M., Brown J., Lehmbeck J.,
RA Clausen I.G.;
RT "Isolation and characterisation of genes for sulphate activation and
RT reduction in Aspergillus nidulans: implications for evolution of an
RT allosteric control region by gene duplication.";
RL Mol. Gen. Genet. 247:423-429(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: The NADP dependent reduction of PAPS into sulfite involves
CC thioredoxin which probably plays the role of a thiol carrier.
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 -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 3/3.
CC -!- SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF76822.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAA60812.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=X82555; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X82555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACD01000080; EAA60812.1; ALT_INIT; Genomic_DNA.
DR EMBL; BN001303; CBF76822.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_662374.1; XM_657282.1.
DR AlphaFoldDB; P56859; -.
DR SMR; P56859; -.
DR STRING; 162425.CADANIAP00005655; -.
DR EnsemblFungi; EAA60812; EAA60812; AN4770.2.
DR GeneID; 2872570; -.
DR KEGG; ani:AN4770.2; -.
DR VEuPathDB; FungiDB:AN4770; -.
DR eggNOG; KOG0189; Eukaryota.
DR HOGENOM; CLU_044089_0_0_1; -.
DR InParanoid; P56859; -.
DR OrthoDB; 834258at2759; -.
DR UniPathway; UPA00140; UER00206.
DR Proteomes; UP000000560; Chromosome III.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; IMP:AspGD.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0000103; P:sulfate assimilation; IMP:AspGD.
DR GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IBA:GO_Central.
DR CDD; cd01713; PAPS_reductase; 1.
DR Gene3D; 3.40.50.620; -; 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 Pfam; PF01507; PAPS_reduct; 1.
DR TIGRFAMs; TIGR00434; cysH; 1.
DR TIGRFAMs; TIGR02057; PAPS_reductase; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cysteine biosynthesis; Methionine biosynthesis;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..306
FT /note="Phosphoadenosine phosphosulfate reductase"
FT /id="PRO_0000100660"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 291..298
FT /note="Missing (in Ref. 1; X82555)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 306 AA; 35447 MW; 433E4C8B05B34955 CRC64;
MPAKMHSNYP SDSETAELRD STESGYVSGG SSEEYLPEIV FTKPHLQFLN RQLQFLEPQD
VLRWCVTSLP HLYQTTAFGL TGLVIMDMLS KLSIPRPQMV NLIFLDTLHH FPETLKLVDN
VRKRYPLQHI HVYKPQGVET EEEFAKKHGE RLWEKDDQLY DWIAKVEPAQ RAYRELNVHA
VLTGRRRSQG GKRGDLDIIE VDEAGLIKIN PLANWTFDQV KQYVKENDIP YNELLDKGYK
SVGDYHSTSP VKENEDERSG RWKGQAKTEC GIHNPRSKYA QYLMDMERKR QEEALSQALQ
NKLTTA
