ID X7E0T2_9GAMM Unreviewed; 301 AA.
AC X7E0T2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
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 ORFNames=MUS1_06955 {ECO:0000313|EMBL:ETX09567.1};
OS Marinomonas ushuaiensis DSM 15871.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=1122207 {ECO:0000313|EMBL:ETX09567.1, ECO:0000313|Proteomes:UP000054058};
RN [1] {ECO:0000313|EMBL:ETX09567.1, ECO:0000313|Proteomes:UP000054058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15871 {ECO:0000313|EMBL:ETX09567.1,
RC ECO:0000313|Proteomes:UP000054058};
RA Lai Q., Shao Z.S.;
RT "Marinomonas ushuaiensis DSM 15871 Genome Sequencing.";
RL Submitted (JAN-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETX09567.1}.
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DR EMBL; JAMB01000019; ETX09567.1; -; Genomic_DNA.
DR RefSeq; WP_036163799.1; NZ_JAMB01000019.1.
DR AlphaFoldDB; X7E0T2; -.
DR STRING; 1122207.MUS1_06955; -.
DR PATRIC; fig|1122207.3.peg.3002; -.
DR eggNOG; COG0175; Bacteria.
DR OrthoDB; 9772604at2; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000054058; 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:ETX09567.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054058};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00064, ECO:0000313|EMBL:ETX09567.1}.
FT DOMAIN 29..255
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; 34677 MW; 281630BCBC87B10A CRC64;
MTEERLTHLK QLEAESIHII REVAAEFDNP VMLYSIGKDS AVMLHLAMKA FYPGKPPFPL
MHVDTTWKFK EMITFRDELV AKLGLELIVH KNQEGIDQGI GPFTHGSSKH TDVMKTQGLK
QALDKYGFDA AFGGARRDEE KSRAKERVYS FRDKQHRWDP KNQRPELWNI YNGKVNKGES
IRVFPLSNWT ELDIWQYIYL ESIPIVPLYF SAKRPVVERD GTMIMVDDER MPLNGEVPEM
KSVRFRTLGC YPLTGAVESE AATLPEIIQE MLLTTSSERE GRMIDHDSSG SMEEKKKQGY
F
//
