ID A9BDJ4_PROM4 Unreviewed; 390 AA.
AC A9BDJ4;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=sulfate adenylyltransferase {ECO:0000256|ARBA:ARBA00012391};
DE EC=2.7.7.4 {ECO:0000256|ARBA:ARBA00012391};
DE AltName: Full=ATP-sulfurylase {ECO:0000256|ARBA:ARBA00041598};
DE AltName: Full=Sulfate adenylate transferase {ECO:0000256|ARBA:ARBA00031812};
GN Name=met3 {ECO:0000313|EMBL:ABX08180.1};
GN OrderedLocusNames=P9211_02491 {ECO:0000313|EMBL:ABX08180.1};
OS Prochlorococcus marinus (strain MIT 9211).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=93059 {ECO:0000313|EMBL:ABX08180.1, ECO:0000313|Proteomes:UP000000788};
RN [1] {ECO:0000313|EMBL:ABX08180.1, ECO:0000313|Proteomes:UP000000788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9211 {ECO:0000313|Proteomes:UP000000788};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(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;
CC Evidence={ECO:0000256|ARBA:ARBA00000262};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3. {ECO:0000256|ARBA:ARBA00005048}.
CC -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family.
CC {ECO:0000256|ARBA:ARBA00037980}.
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DR EMBL; CP000878; ABX08180.1; -; Genomic_DNA.
DR RefSeq; WP_012194805.1; NC_009976.1.
DR AlphaFoldDB; A9BDJ4; -.
DR STRING; 93059.P9211_02491; -.
DR KEGG; pmj:P9211_02491; -.
DR eggNOG; COG2046; Bacteria.
DR HOGENOM; CLU_022950_1_0_3; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000000788; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-EC.
DR GO; GO:0000103; P:sulfate assimilation; IEA:InterPro.
DR CDD; cd00517; ATPS; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.10.400.10; Sulfate adenylyltransferase; 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; IPR024951; Sulfurylase_cat_dom.
DR InterPro; IPR002650; Sulphate_adenylyltransferase.
DR NCBIfam; TIGR00339; sopT; 1.
DR PANTHER; PTHR43509; -; 1.
DR PANTHER; PTHR43509:SF1; SULFATE ADENYLYLTRANSFERASE; 1.
DR Pfam; PF01747; ATP-sulfurylase; 1.
DR Pfam; PF14306; PUA_2; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:ABX08180.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000788};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABX08180.1}.
FT DOMAIN 15..166
FT /note="ATP-sulfurylase PUA-like"
FT /evidence="ECO:0000259|Pfam:PF14306"
FT DOMAIN 176..389
FT /note="Sulphate adenylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01747"
SQ SEQUENCE 390 AA; 44210 MW; 396741038B566CF4 CRC64;
MTSNQSHPKR QSEVIAPYGG SLVDLMLPKA DQEKVKKNVR GKLECSDRNA CDIELLVIGG
FSPLRGFMLK DDYESVIKNH RTTSGDLFGL PIVMDTDRED LVIGDQVLLT YKGQDIAVLK
IEEKWEPDKM LEAKGCYGTT SLEHPAVRMI AMQRKRFYLG GAVHGLELPK RVFPCKTPAE
LRKELPKDED VVAFQCRNPI HRAHYELFTR ALDADNVSKN AVVLVHPTCG PTQEDDIAGE
VRFQTYERLA SEVNNPRIKW AYLPYSMHMA GPREALQHMI IRRNYGCTHF IIGRDMAGCK
SSLNGDDFYG PYEAQDFAKK YSTELSMDTV PSLNLVFTEE EGYVTAEHAK SCNLHIKKLS
GTEFRKMLRN GEDIPEWFAF KSVVEVLRKA
//
