ID G0A332_METMM Unreviewed; 302 AA.
AC G0A332;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
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 OrderedLocusNames=Metme_0520 {ECO:0000313|EMBL:AEF98964.1};
OS Methylomonas methanica (strain MC09).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=857087 {ECO:0000313|EMBL:AEF98964.1, ECO:0000313|Proteomes:UP000008888};
RN [1] {ECO:0000313|EMBL:AEF98964.1, ECO:0000313|Proteomes:UP000008888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC09 {ECO:0000313|EMBL:AEF98964.1,
RC ECO:0000313|Proteomes:UP000008888};
RX PubMed=22123758; DOI=10.1128/JB.06267-11;
RA Boden R., Cunliffe M., Scanlan J., Moussard H., Kits K.D., Klotz M.G.,
RA Jetten M.S., Vuilleumier S., Han J., Peters L., Mikhailova N., Teshima H.,
RA Tapia R., Kyrpides N., Ivanova N., Pagani I., Cheng J.F., Goodwin L.,
RA Han C., Hauser L., Land M.L., Lapidus A., Lucas S., Pitluck S., Woyke T.,
RA Stein L., Murrell J.C.;
RT "Complete Genome Sequence of the Aerobic Marine Methanotroph Methylomonas
RT methanica MC09.";
RL J. Bacteriol. 193:7001-7002(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MC09;
RA Boden R., Cunliffe M., Scanlan J., Moussard H., Kits K.D., Klotz M.,
RA Jetten M., Vuilleumier S., Han J., Peters L., Mikhailova N., Teshima H.,
RA Tapia R., Kyrpides N., Ivanova N., Pagani I., Cheng J.-F., Goodwin L.,
RA Han C., Hauser L., Land M., Lapidus A., Lucas S., Pitluck S., Woyke T.,
RA Stein L.Y., Murrell C.;
RT "Complete genome sequence of the aerobic marine methanotroph Methylomonas
RT methanica MC09.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000008888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC09 {ECO:0000313|Proteomes:UP000008888};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Stein L., Woyke T.;
RT "Complete sequence of Methylomonas methanica MC09.";
RL Submitted (MAY-2011) 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; CP002738; AEF98964.1; -; Genomic_DNA.
DR RefSeq; WP_013817235.1; NC_015572.1.
DR AlphaFoldDB; G0A332; -.
DR STRING; 857087.Metme_0520; -.
DR KEGG; mmt:Metme_0520; -.
DR eggNOG; COG0175; Bacteria.
DR HOGENOM; CLU_043026_0_0_6; -.
DR OrthoDB; 9772604at2; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000008888; 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:AEF98964.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008888};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00064, ECO:0000313|EMBL:AEF98964.1}.
FT DOMAIN 30..256
FT /note="Phosphoadenosine phosphosulphate reductase"
FT /evidence="ECO:0000259|Pfam:PF01507"
SQ SEQUENCE 302 AA; 35178 MW; 74473F8572944ECA CRC64;
MTDYKLTHLK QLEAESIHII REVAAEFDKP VMLYSIGKDS AVMLHLTRKA FFPGKPPFPL
LHVDTTWKFK EMIEFRNRMA EDLGWDLMVH INQDGVEQGI GPFTHGSKKH TDVMKTDALK
QALNKHQFDA AFGGARRDEE KSRAKERVYS FRDKNHRWDP KNQRPELWNI YNGKVEKGES
IRVFPLSNWT ELDIWQYIHL ENIPIVPLYF AKERPVVEKD GMLIMVDDER MPIGPDDKIE
MKMVRFRTLG CYPLTGAVES TATTLPEIIQ EMLLTTTSER QGRLIDHDQA GSMEQKKREG
YF
//
