ID A0A085U393_YERRU Unreviewed; 302 AA.
AC A0A085U393;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
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:SUQ00113.1};
GN ORFNames=CSF007_3600 {ECO:0000313|EMBL:CEK26499.1}, NCTC10476_01387
GN {ECO:0000313|EMBL:SUQ00113.1};
OS Yersinia ruckeri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=29486 {ECO:0000313|EMBL:CEK26499.1};
RN [1] {ECO:0000313|EMBL:CEK26499.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CSF007-82 {ECO:0000313|EMBL:CEK26499.1};
RA Nelson M.C., LaPatra S.E., Welch T.J., Graf J.;
RT "Complete Genome Sequence of Yersinia ruckeri Strain CSF007-82, Etiologic
RT Agent of Red Mouth Disease in Salmonid Fish.";
RL Genome Announc. 3:1-2(2015).
RN [2] {ECO:0000313|EMBL:SUQ00113.1, ECO:0000313|Proteomes:UP000255169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10476 {ECO:0000313|EMBL:SUQ00113.1,
RC ECO:0000313|Proteomes:UP000255169};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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; 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; LN681231; CEK26499.1; -; Genomic_DNA.
DR EMBL; UHJG01000001; SUQ00113.1; -; Genomic_DNA.
DR RefSeq; WP_004719142.1; NZ_VDHI01000015.1.
DR AlphaFoldDB; A0A085U393; -.
DR STRING; 29486.UGYR_13530; -.
DR GeneID; 66878476; -.
DR KEGG; yrb:UGYR_13530; -.
DR PATRIC; fig|29486.44.peg.3223; -.
DR eggNOG; COG0175; Bacteria.
DR OrthoDB; 9772604at2; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000255169; Unassembled WGS sequence.
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:CEK26499.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000255169};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00064, ECO:0000313|EMBL:CEK26499.1}.
FT DOMAIN 29..256
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
SQ SEQUENCE 302 AA; 35145 MW; B3E816EB713DED74 CRC64;
MDEKRLTHLR QLEAESIHII REVAAEFGNP VMLYSIGKDS SVMLHLARKA FFPGNLPFPL
LHVDTGWKFR EMYQFRDDTV KAFGCKLLVH RNPEGVAMGI NPFKHGSAKH TDIMKTEGLK
QALNKYGFDA AFGGARRDEE KSRAKERIYS FRDRFHRWDP KNQRPELWHN YNGQINKGES
IRVFPLSNWT ELDIWQYIFL ENIEIVPLYL AKPRPVIERD GMLLMVDDDR IDLQPGEVIT
QKMVRFRTLG CWPLTGAVES QAETLPTIIE EMLISTTSER QGRMIDRDQS GSMELKKRQG
YF
//
