CYSD_PSESM
ID CYSD_PSESM Reviewed; 305 AA.
AC Q87WW0;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Sulfate adenylyltransferase subunit 2 {ECO:0000255|HAMAP-Rule:MF_00064};
DE EC=2.7.7.4 {ECO:0000255|HAMAP-Rule:MF_00064};
DE AltName: Full=ATP-sulfurylase small subunit {ECO:0000255|HAMAP-Rule:MF_00064};
DE AltName: Full=Sulfate adenylate transferase {ECO:0000255|HAMAP-Rule:MF_00064};
DE Short=SAT {ECO:0000255|HAMAP-Rule:MF_00064};
GN Name=cysD {ECO:0000255|HAMAP-Rule:MF_00064}; OrderedLocusNames=PSPTO_4433;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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:0000255|HAMAP-Rule:MF_00064}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + sulfate = 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:0000255|HAMAP-
CC Rule:MF_00064};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3. {ECO:0000255|HAMAP-Rule:MF_00064}.
CC -!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and CysN.
CC {ECO:0000255|HAMAP-Rule:MF_00064}.
CC -!- SIMILARITY: Belongs to the PAPS reductase family. CysD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00064}.
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DR EMBL; AE016853; AAO57882.1; -; Genomic_DNA.
DR RefSeq; NP_794187.1; NC_004578.1.
DR RefSeq; WP_003313577.1; NC_004578.1.
DR PDB; 1ZUN; X-ray; 2.70 A; A=1-305.
DR PDBsum; 1ZUN; -.
DR AlphaFoldDB; Q87WW0; -.
DR SMR; Q87WW0; -.
DR STRING; 223283.PSPTO_4433; -.
DR EnsemblBacteria; AAO57882; AAO57882; PSPTO_4433.
DR GeneID; 61790762; -.
DR GeneID; 64445170; -.
DR GeneID; 65076789; -.
DR KEGG; pst:PSPTO_4433; -.
DR PATRIC; fig|223283.9.peg.4548; -.
DR eggNOG; COG0175; Bacteria.
DR HOGENOM; CLU_043026_0_0_6; -.
DR OMA; LMIDTGH; -.
DR OrthoDB; 499077at2; -.
DR PhylomeDB; Q87WW0; -.
DR UniPathway; UPA00140; UER00204.
DR EvolutionaryTrace; Q87WW0; -.
DR Proteomes; UP000002515; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; ISS:JCVI.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR GO; GO:0019419; P:sulfate reduction; IEA:InterPro.
DR GO; GO:0006790; P:sulfur compound metabolic process; ISS:JCVI.
DR CDD; cd01713; PAPS_reductase; 1.
DR DisProt; DP00985; -.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00064; Sulf_adenylyltr_sub2; 1.
DR InterPro; IPR002500; PAPS_reduct.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR011784; SO4_adenylTrfase_ssu.
DR Pfam; PF01507; PAPS_reduct; 1.
DR PIRSF; PIRSF002936; CysDAde_trans; 1.
DR TIGRFAMs; TIGR02039; CysD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..305
FT /note="Sulfate adenylyltransferase subunit 2"
FT /id="PRO_0000100671"
FT HELIX 7..25
FT /evidence="ECO:0007829|PDB:1ZUN"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:1ZUN"
FT HELIX 37..50
FT /evidence="ECO:0007829|PDB:1ZUN"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1ZUN"
FT HELIX 69..80
FT /evidence="ECO:0007829|PDB:1ZUN"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1ZUN"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:1ZUN"
FT HELIX 108..113
FT /evidence="ECO:0007829|PDB:1ZUN"
FT HELIX 115..125
FT /evidence="ECO:0007829|PDB:1ZUN"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:1ZUN"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:1ZUN"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:1ZUN"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:1ZUN"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:1ZUN"
FT TURN 184..187
FT /evidence="ECO:0007829|PDB:1ZUN"
FT HELIX 190..200
FT /evidence="ECO:0007829|PDB:1ZUN"
SQ SEQUENCE 305 AA; 35312 MW; C34C7ECA9448552F CRC64;
MVDKLTHLKQ LEAESIHIIR EVAAEFDNPV MLYSIGKDSA VMLHLARKAF FPGKLPFPVM
HVDTRWKFQE MYRFRDQMVE EMGLDLITHI NPDGVAQGIN PFTHGSAKHT DIMKTEGLKQ
ALDKHGFDAA FGGARRDEEK SRAKERVYSF RDSKHRWDPK NQRPELWNVY NGNVNKGESI
RVFPLSNWTE LDIWQYIYLE GIPIVPLYFA AERDVIEKNG TLIMIDDERI LEHLTDEEKS
RIVKKKVRFR TLGCYPLTGA VESEATSLTD IIQEMLLTRT SERQGRVIDH DGAGSMEEKK
RQGYF
