APR1_ORYSJ
ID APR1_ORYSJ Reviewed; 475 AA.
AC Q6Z4A7;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Probable 5'-adenylylsulfate reductase 1, chloroplastic;
DE EC=1.8.4.9;
DE AltName: Full=Adenosine 5'-phosphosulfate 5'-adenylylsulfate sulfotransferase 1;
DE Short=APS sulfotransferase 1;
DE AltName: Full=Adenosine 5'-phosphosulfate reductase-like 1;
DE Short=APR-like1;
DE Short=OsAPRL1;
DE AltName: Full=Thioredoxin-independent APS reductase 1;
DE Flags: Precursor;
GN Name=APR1; OrderedLocusNames=Os07g0509800, LOC_Os07g32570;
GN ORFNames=P0409B11.14;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
CC -!- FUNCTION: Reduces sulfate for Cys biosynthesis. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + glutathione disulfide + 2 H(+) + sulfite = adenosine 5'-
CC phosphosulfate + 2 glutathione; Xref=Rhea:RHEA:14141,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58243, ChEBI:CHEBI:58297, ChEBI:CHEBI:456215; EC=1.8.4.9;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- DOMAIN: The C-terminal domain may function as glutaredoxin and mediates
CC the interaction of the enzyme with glutathione (GSH). Active in GSH-
CC dependent reduction of hydroxyethyldisulfide, cystine,
CC dehydroascorbate, insulin disulfides and ribonucleotide reductase.
CC -!- SIMILARITY: Belongs to the APS reductase family. {ECO:0000305}.
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DR EMBL; AP005185; BAC83952.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF21664.1; -; Genomic_DNA.
DR EMBL; AP014963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015647625.1; XM_015792139.1.
DR AlphaFoldDB; Q6Z4A7; -.
DR SMR; Q6Z4A7; -.
DR BioGRID; 812385; 1.
DR STRING; 4530.OS07T0509800-01; -.
DR PaxDb; Q6Z4A7; -.
DR PRIDE; Q6Z4A7; -.
DR GeneID; 4343348; -.
DR KEGG; osa:4343348; -.
DR eggNOG; KOG0189; Eukaryota.
DR eggNOG; KOG0191; Eukaryota.
DR HOGENOM; CLU_044089_4_0_1; -.
DR InParanoid; Q6Z4A7; -.
DR OrthoDB; 834258at2759; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR Genevisible; Q6Z4A7; OS.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0033741; F:adenylyl-sulfate reductase (glutathione) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0019419; P:sulfate reduction; IEA:InterPro.
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; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR004508; Thioredoxin-indep_APS_Rdtase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF01507; PAPS_reduct; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR00424; APS_reduc; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Amino-acid biosynthesis; Chloroplast; Cysteine biosynthesis;
KW Disulfide bond; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Plastid;
KW Redox-active center; Reference proteome; Stress response; Transit peptide.
FT TRANSIT 1..63
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 64..475
FT /note="Probable 5'-adenylylsulfate reductase 1,
FT chloroplastic"
FT /id="PRO_0000400040"
FT DOMAIN 341..475
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 72..327
FT /note="Reductase domain"
FT /evidence="ECO:0000250"
FT ACT_SITE 393
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 396
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT DISULFID 393..396
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 475 AA; 50591 MW; 0A5BDF8F9B5C2531 CRC64;
MASATASISS HSVALRDLKA ARIGAVKQQV AAAPAAGTAA ARAQRARAVR PLRAAEPARQ
PVSASAAAAP AAAPVAEDAA AAAVDAPAPA VDYEALAQEL QGASPLEIMD RALAMFGSDI
AIAFSGAEDV ALIEYAKLTG RPFRVFSLDT GRLNPETYQL FDKVEKHYGI RIEYMFPDAG
EVQALVRAKG LFSFYEDGHQ ECCRARKVRP LRRALRGLRA WITGQRKDQS PGTRAAIPVV
QVDPSFEGLA GGAGSLVKWN PVANVDGKDV WTFLRAMDVP VNALHAQGYV SIGCEPCTRP
VLPGQHEREG RWWWEDAKAK ECGLHKGNID DQGGAAAAAA HKAGGANGNG SAGAPDIFES
SGVVSLTRAG VENLLRLESR AEPWLVVLYA PWCPFCQAME ASYLELAERL GGAGGGVKVG
KFRADGEQKA FAQQELQLQS FPTILLFPSR TARPIKYPSE KRDVDSLLAF VNSLR
