ID   B2AIS1_CUPTR            Unreviewed;       298 AA.
AC   B2AIS1;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   02-SEP-2026, entry version 111.
DE   RecName: Full=Sulfate adenylyltransferase subunit 2 {ECO:0000256|HAMAP-Rule:MF_00064};
DE            EC=2.7.7.4 {ECO:0000256|HAMAP-Rule:MF_00064};
DE   AltName: Full=ATP-sulfurylase small subunit {ECO:0000256|HAMAP-Rule:MF_00064};
DE   AltName: Full=Sulfate adenylate transferase {ECO:0000256|HAMAP-Rule:MF_00064};
DE            Short=SAT {ECO:0000256|HAMAP-Rule:MF_00064};
GN   Name=cysD1 {ECO:0000313|EMBL:CAP63670.1};
GN   Synonyms=cysD {ECO:0000256|HAMAP-Rule:MF_00064};
GN   OrderedLocusNames=RALTA_B0476 {ECO:0000313|EMBL:CAP63670.1};
OS   Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS   107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=977880 {ECO:0000313|EMBL:CAP63670.1, ECO:0000313|Proteomes:UP000001692};
RN   [1] {ECO:0000313|EMBL:CAP63670.1, ECO:0000313|Proteomes:UP000001692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 /
RC   R1 {ECO:0000313|Proteomes:UP000001692};
RX   PubMed=18490699; DOI=10.1101/gr.076448.108;
RA   Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA   Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA   Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA   Masson-Boivin C.;
RT   "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT   comparative genomics of rhizobia.";
RL   Genome Res. 18:1472-1483(2008).
CC   -!- FUNCTION: With CysN forms the ATP sulfurylase (ATPS) that catalyzes the
CC       adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and
CC       diphosphate, the first enzymatic step in sulfur assimilation pathway.
CC       APS synthesis involves the formation of a high-energy phosphoric-
CC       sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled
CC       to ATP hydrolysis by CysD. {ECO:0000256|HAMAP-Rule:MF_00064}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=sulfate + ATP + H(+) = adenosine 5'-phosphosulfate +
CC         diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58243; EC=2.7.7.4; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00064};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 1/3. {ECO:0000256|HAMAP-Rule:MF_00064}.
CC   -!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and CysN.
CC       {ECO:0000256|HAMAP-Rule:MF_00064}.
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. CysD subfamily.
CC       {ECO:0000256|ARBA:ARBA00008885, ECO:0000256|HAMAP-Rule:MF_00064}.
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DR   EMBL; CU633750; CAP63670.1; -; Genomic_DNA.
DR   RefSeq; WP_012355323.1; NC_010530.1.
DR   AlphaFoldDB; B2AIS1; -.
DR   GeneID; 29764782; -.
DR   KEGG; cti:RALTA_B0476; -.
DR   eggNOG; COG0175; Bacteria.
DR   HOGENOM; CLU_043026_0_0_4; -.
DR   BioCyc; CTAI977880:RALTA_RS18035-MONOMER; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000001692; Chromosome 2.
DR   GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR   CDD; cd23946; Sulfate_adenylyltransferase_2; 1.
DR   FunFam; 3.40.50.620:FF:000002; Sulfate adenylyltransferase subunit 2; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00064; Sulf_adenylyltr_sub2; 1.
DR   InterPro; IPR002500; PAPS_reduct_dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011784; SO4_adenylTrfase_ssu.
DR   InterPro; IPR050128; Sulfate_adenylyltrnsfr_sub2.
DR   NCBIfam; TIGR02039; CysD; 1.
DR   NCBIfam; NF003587; PRK05253.1; 1.
DR   NCBIfam; NF009214; PRK12563.1; 1.
DR   PANTHER; PTHR43196; SULFATE ADENYLYLTRANSFERASE SUBUNIT 2; 1.
DR   PANTHER; PTHR43196:SF1; SULFATE ADENYLYLTRANSFERASE SUBUNIT 2; 1.
DR   Pfam; PF01507; PAPS_reduct; 1.
DR   PIRSF; PIRSF002936; CysDAde_trans; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00064};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00064};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00064}; Reference proteome {ECO:0000313|Proteomes:UP000001692};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00064}.
FT   DOMAIN          25..252
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
FT   REGION          275..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..298
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   298 AA;  34489 MW;  E31F7FC956E5646A CRC64;
     MLTHLEQLEA ESIHIMREVV AECENPVMLY SIGKDSAVML HLAMKAFHPA RPPFPLLHVD
     TTWKFREMIA FRDQTAARLG LDLRVHINPE GLARKISPHE HGSAVHTDVW KTQGLKQALD
     HYGFDAAFGG ARRDEEKSRA KERVFSVRTA QHRWDPKMQR PELWRQYNTR KRKGESLRVF
     PLSNWTELDI WQYIYLNEIP IVPLYFARER PVVERDGTLI MVDDERLPLR PGETPQLRKV
     RFRTLGCYPL TGAIESEADT LGGIIQEMLR ATTSERQGRL IDSDSAGSME KKKQEGYF
//