ID A0A0A7PFR1_9SPHN Unreviewed; 301 AA.
AC A0A0A7PFR1;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=cysD {ECO:0000256|HAMAP-Rule:MF_00064,
GN ECO:0000313|EMBL:AJA08956.1};
GN ORFNames=SKP52_10250 {ECO:0000313|EMBL:AJA08956.1};
OS Sphingopyxis fribergensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1515612 {ECO:0000313|EMBL:AJA08956.1, ECO:0000313|Proteomes:UP000030907};
RN [1] {ECO:0000313|EMBL:AJA08956.1, ECO:0000313|Proteomes:UP000030907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kp5.2 {ECO:0000313|EMBL:AJA08956.1,
RC ECO:0000313|Proteomes:UP000030907};
RX PubMed=26040579; DOI=10.1099/ijs.0.000371;
RA Oelschlagel M., Ruckert C., Kalinowski J., Schmidt G., Schlomann M.,
RA Tischler D.;
RT "Description of Sphingopyxis fribergensis sp. nov. - a soil bacterium with
RT the ability to degrade styrene and phenylacetic acid.";
RL Int. J. Syst. Evol. Microbiol. 65:3008-3015(2015).
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=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;
CC Evidence={ECO:0000256|ARBA:ARBA00000262, 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; CP009122; AJA08956.1; -; Genomic_DNA.
DR RefSeq; WP_039574500.1; NZ_CP009122.1.
DR AlphaFoldDB; A0A0A7PFR1; -.
DR STRING; 1515612.SKP52_10250; -.
DR KEGG; sphk:SKP52_10250; -.
DR HOGENOM; CLU_043026_0_0_5; -.
DR OrthoDB; 9772604at2; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000030907; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-UniRule.
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 CDD; cd01713; PAPS_reductase; 1.
DR Gene3D; 3.40.50.620; HUPs; 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 NCBIfam; TIGR02039; CysD; 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|HAMAP-Rule:MF_00064};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00064};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00064,
KW ECO:0000313|EMBL:AJA08956.1};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00064, ECO:0000313|EMBL:AJA08956.1}.
FT DOMAIN 29..254
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
FT REGION 278..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 301 AA; 34512 MW; 99F8DC9D523CC697 CRC64;
MIDTLTHLDR LEAESIHIMR EVMADAAKPV MLYSVGKDSA VMLHLARKAF YPSPPPFPLL
HVDTTWKFQA MYELRDRMAA ESGMELIVYQ NPEAKERGIN PFDHGPLHTD MWKTEGLKQA
LDLHGFDVAF GGARRDEEKS RAKERIFSFR TASHGWDPKK QRPELWNLYN ARKAKGESIR
VFPISNWTEL DIWQYIAREN IPIVPLYFAA PRPTVERDGL LLMVDDDRFP LLPGETPVER
SVRFRTLGCY PLTGAVESEA KTLSEVIQEM LLTTTSERQG RIIDKDGGDA SMEKKKQEGY
F
//
