ID A0A1E4KC96_9PROT Unreviewed; 405 AA.
AC A0A1E4KC96;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 ORFNames=ABS92_14245 {ECO:0000313|EMBL:ODU37510.1};
OS Thiobacillus sp. SCN 63-374.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=1660149 {ECO:0000313|EMBL:ODU37510.1, ECO:0000313|Proteomes:UP000094238};
RN [1] {ECO:0000313|EMBL:ODU37510.1, ECO:0000313|Proteomes:UP000094238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODU37510.1}.
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DR EMBL; MEFK01000243; ODU37510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4KC96; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000094238; Unassembled WGS sequence.
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 6..164
FT /note="ATP-sulfurylase PUA-like"
FT /evidence="ECO:0000259|Pfam:PF14306"
FT DOMAIN 176..385
FT /note="Sulphate adenylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01747"
SQ SEQUENCE 405 AA; 44273 MW; D4911A33BDA17181 CRC64;
MSKLVRPHGG GELKPLLLTG AALAAEQARA ASLPKVKMTS RETGDLIMMG IGGFTPLEGF
MTHADWQGVC DGYKMANGLF WPIPVTLSAD EVTAQNIAVG ADIALVDSES GNIMGTMKVT
EKYAIDKAHE CMQVYKTTDL EHPGVKMVMD QGPVNLAGPV KVLSTGNFKE EYGDQFMTPA
ETRAAFEKMG WSKIAAFQTR NPMHRSHEYL AKIAIETMDG VLIHSLLGAL KPGDIPAEVR
SEAIATLIDN YFAPNTVIQA GYPLDMRYAG PREALLHALF RQNYGCSHLI VGRDHAGVGD
YYGPFDAQKI FDEIPKDALE TKNMNIDWTF WCNKCGGMAS QRTCPHTKDD RILLSGTKVR
SMLSEGQDLP VEFSRPEVAK VLQKYYAGLS AEQNVKVELK GHSAA
//
