SAT_PELPB
ID SAT_PELPB Reviewed; 403 AA.
AC B4SAM9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 73.
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=Ppha_0041;
OS Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Pelodictyon.
OX NCBI_TaxID=324925;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5477 / BU-1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Pelodictyon phaeoclathratiforme BU-1.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001110; ACF42398.1; -; Genomic_DNA.
DR RefSeq; WP_012506896.1; NC_011060.1.
DR AlphaFoldDB; B4SAM9; -.
DR SMR; B4SAM9; -.
DR STRING; 324925.Ppha_0041; -.
DR EnsemblBacteria; ACF42398; ACF42398; Ppha_0041.
DR KEGG; pph:Ppha_0041; -.
DR eggNOG; COG2046; Bacteria.
DR HOGENOM; CLU_022950_1_1_10; -.
DR OMA; LQHMIIR; -.
DR OrthoDB; 1574819at2; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000002724; 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..403
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_1000092260"
SQ SEQUENCE 403 AA; 45046 MW; 937EE7674FEC2F1B CRC64;
MSLVNPHGRE KILKPLLLSG QALQNEQERA KSMARVTLSS RETGDLIMLG IGGFTPLSGF
MGYEDWKGSV EECKLADGTF WPIPITLSTT KEQADKLKIG AEVALVDEES GETMGSMTIE
EKYAIDKSHE CREVFKTDDP KHPGVLMVMN QGDVNLGGSV KVFSEGSFPS EFEGIYMTPA
QTRKMFEDNG WSTVAAFQTR NPMHRSHEYL VKIAIEICDG VLIHQLLGKL KPGDIPADVR
RDCINVLMDN YFVKGTCIQG GYPLDMRYAG PREALLHALF RQNFGCSHLI VGRDHAGVGD
YYGPFDAHYI FDQIPKDALE TKPLKIDWTF YCYKCDGMAS MKTCPHTNED RLNVSGTKLR
KMLSEGEEVP EHFSRPEVLE VLHRYYATLT EKVDIGLQTN TGG
