ID A0A160IKK2_9BACI Unreviewed; 376 AA.
AC A0A160IKK2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Sulfate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00066};
DE EC=2.7.7.4 {ECO:0000256|HAMAP-Rule:MF_00066};
DE AltName: Full=ATP-sulfurylase {ECO:0000256|HAMAP-Rule:MF_00066};
DE AltName: Full=Sulfate adenylate transferase {ECO:0000256|HAMAP-Rule:MF_00066};
DE Short=SAT {ECO:0000256|HAMAP-Rule:MF_00066};
GN Name=sat {ECO:0000256|HAMAP-Rule:MF_00066,
GN ECO:0000313|EMBL:ANC76683.1};
GN ORFNames=ABE65_007660 {ECO:0000313|EMBL:ANC76683.1};
OS Fictibacillus phosphorivorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=1221500 {ECO:0000313|EMBL:ANC76683.1, ECO:0000313|Proteomes:UP000076623};
RN [1] {ECO:0000313|EMBL:ANC76683.1, ECO:0000313|Proteomes:UP000076623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25-29 {ECO:0000313|EMBL:ANC76683.1,
RC ECO:0000313|Proteomes:UP000076623};
RA Zheng Z.;
RT "Complete genome sequence of Fictibacillus phosphorivorans G25-29, a strain
RT toxic to nematodes.";
RL Submitted (APR-2016) 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;
CC Evidence={ECO:0000256|ARBA:ARBA00000262, ECO:0000256|HAMAP-
CC Rule:MF_00066};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3. {ECO:0000256|ARBA:ARBA00005048, ECO:0000256|HAMAP-
CC Rule:MF_00066}.
CC -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family.
CC {ECO:0000256|ARBA:ARBA00037980, ECO:0000256|HAMAP-Rule:MF_00066}.
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DR EMBL; CP015378; ANC76683.1; -; Genomic_DNA.
DR RefSeq; WP_066393196.1; NZ_CP015378.1.
DR AlphaFoldDB; A0A160IKK2; -.
DR STRING; 1221500.ABE65_007660; -.
DR KEGG; fpn:ABE65_007660; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000076623; 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; HUPs; 1.
DR Gene3D; 3.10.400.10; Sulfate adenylyltransferase; 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 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, ECO:0000256|HAMAP-
KW Rule:MF_00066};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00066};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00066};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00066}.
FT DOMAIN 5..153
FT /note="ATP-sulfurylase PUA-like"
FT /evidence="ECO:0000259|Pfam:PF14306"
FT DOMAIN 162..372
FT /note="Sulphate adenylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01747"
SQ SEQUENCE 376 AA; 42953 MW; 922F5F21DAC26CA1 CRC64;
MLLLPHGGSL VNRQFTNVEC NQNQIKIELD AISLSDLECI SNGAFSPLDS FMNKADYESV
VNGMRLYNGL PWSVPITLPV TDDKAKQLIK QQEALLIYEN TVYGKIEITD IYKPDKLLEV
KNVYRTEDVS HPGVQNVLNR GSWYVGGKVT LVNKPPRKVD SSYYLNPKET REQFNKNGWE
KIVGFQTRNP IHRAHEYLQK TALEQMDGLL LHPLVGETKQ DDIPAEVRMK SYETLLQHYY
PKNRVLLGAF PGSMRYAGPR EAIFHSIIRK NYGCSHIIIG RDHAGVGNFY GPYDAQHIFA
EFNKEEIGIT PIFFENSFYC TKCGAMATIK TCPHDEKDRL ILSGTKVREM LKNNEPISPH
FSRNEVISIL RDYYGE
//