ID A0A268U3K2_9HELI Unreviewed; 392 AA.
AC A0A268U3K2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Sulfate adenylyltransferase {ECO:0000313|EMBL:PAF51579.1};
GN ORFNames=BKH44_05010 {ECO:0000313|EMBL:PAF51579.1};
OS Helicobacter sp. 13S00477-4.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1905759 {ECO:0000313|EMBL:PAF51579.1, ECO:0000313|Proteomes:UP000216315};
RN [1] {ECO:0000313|EMBL:PAF51579.1, ECO:0000313|Proteomes:UP000216315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13S00477-4 {ECO:0000313|EMBL:PAF51579.1,
RC ECO:0000313|Proteomes:UP000216315};
RX PubMed=28827684; DOI=10.1038/s41598-017-09091-7;
RA Gilbert M.J., Duim B., Timmerman A.J., Zomer A.L., Wagenaar J.A.;
RT "Whole genome-based phylogeny of reptile-associated Helicobacter indicates
RT independent niche adaptation followed by diversification in a
RT poikilothermic host.";
RL Sci. Rep. 7:8387-8387(2017).
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3. {ECO:0000256|ARBA:ARBA00005048}.
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:PAF51579.1}.
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DR EMBL; MLAS01000008; PAF51579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A268U3K2; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000216315; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:InterPro.
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 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:PAF51579.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PAF51579.1}.
FT DOMAIN 7..137
FT /note="ATP-sulfurylase PUA-like"
FT /evidence="ECO:0000259|Pfam:PF14306"
FT DOMAIN 140..347
FT /note="Sulphate adenylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01747"
SQ SEQUENCE 392 AA; 45398 MW; 18B7A8B924ADF8AE CRC64;
MASLERNKIY IDKEALSALS LVQEGLLYPV NKLMRQDEMQ EVNASGLYKN YSFPCPFILS
PSGRRNQEVL SKVKKGETLD IVSEDKIVGM ITADEIYKID KLQRLEKIMG GDLSTQEAVF
TLQRLGDYAI SGEFNVVFDD IRVAKEALQS KIKLLGAKKI TGVMMSAKPF HRAHERMLRE
ELDHCDLLVI FLLKPYKKDL MDFHLREKCM QYIANHFLIK DKICIIALDD TYLFAGQNKM
ILHAIVAKNY GCTKLIVGQN TPNLSIYYTD NERHSIFDRL QGVEIETQII SEYVYCAYCK
MLVSKSTCPH GYHHHTNYNT HSILQLLRVG ILPPSILMRE QISAMILSSF FPNRFENLER
LYYDLVPSEG ILNNRDEEEF YVKLMQLYQI YR
//
