SAT_MICAN
ID SAT_MICAN Reviewed; 389 AA.
AC B0JW81;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Sulfate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00066};
DE EC=2.7.7.4 {ECO:0000255|HAMAP-Rule:MF_00066};
DE AltName: Full=ATP-sulfurylase {ECO:0000255|HAMAP-Rule:MF_00066};
DE AltName: Full=Sulfate adenylate transferase {ECO:0000255|HAMAP-Rule:MF_00066};
DE Short=SAT {ECO:0000255|HAMAP-Rule:MF_00066};
GN Name=sat {ECO:0000255|HAMAP-Rule:MF_00066}; OrderedLocusNames=MAE_17390;
OS Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Microcystaceae; Microcystis.
OX NCBI_TaxID=449447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-843 / IAM M-247;
RX PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT Microcystis aeruginosa NIES-843.";
RL DNA Res. 14:247-256(2007).
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_00066};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3. {ECO:0000255|HAMAP-Rule:MF_00066}.
CC -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_00066}.
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DR EMBL; AP009552; BAG01561.1; -; Genomic_DNA.
DR RefSeq; WP_002803711.1; NC_010296.1.
DR AlphaFoldDB; B0JW81; -.
DR SMR; B0JW81; -.
DR STRING; 449447.MAE_17390; -.
DR PaxDb; B0JW81; -.
DR EnsemblBacteria; BAG01561; BAG01561; MAE_17390.
DR GeneID; 66708559; -.
DR KEGG; mar:MAE_17390; -.
DR eggNOG; COG2046; Bacteria.
DR HOGENOM; CLU_022950_1_1_3; -.
DR OMA; LQHMIIR; -.
DR OrthoDB; 1574819at2; -.
DR BioCyc; MAER449447:MAE_RS07615-MON; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000001510; 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 CDD; cd00517; ATPS; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00066; Sulf_adenylyltr; 1.
DR InterPro; IPR025980; ATP-Sase_PUA-like_dom.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR020792; SO4_adenylyltransferase_pro.
DR InterPro; IPR024951; Sulfurylase_cat_dom.
DR InterPro; IPR002650; Sulphate_adenylyltransferase.
DR Pfam; PF01747; ATP-sulfurylase; 1.
DR Pfam; PF14306; PUA_2; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00339; sopT; 1.
PE 3: Inferred from homology;
KW ATP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..389
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_0000340625"
SQ SEQUENCE 389 AA; 44084 MW; ADB2DD496123013E CRC64;
MTVLTEGIAP HGGQLINRIA TAAEKAEFLA LAEKLPRVSL DERALSDLVM IAIGGFSPLK
GFMEQDDYEK VVDDMRLING LPWAIPVTLS VREEVADPLK EGNWIRLDDS EGNFVGVLEL
TQKYRYNKAH EAVNVYRTDD QKHPGVKVLY EQGEINLAGP IWLLQRDPHP QFPKYQIDPL
QSRKMFHEKA WKTIVGFQTR NPIHRAHEYI QKCALEVVDG LFLHPLVGAT KSDDVPADVR
MRCYEIMMDK YFPQDRVILA INPSAMRYAG PREAIFHAII RKNYGCTHFI VGRDHAGVGD
YYGTYDAQYI FDEFEPGELG IVPMKFEHAF YCTRTSGMAT TKTSPSLPEE RIHLSGTKVR
ELLRKGELPP PEFSRPEVAA ELIRAMQGS