ID A0A1G1JQ77_9BACT Unreviewed; 371 AA.
AC A0A1G1JQ77;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Adenylyl-sulfate kinase {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000256|RuleBase:RU004347};
DE EC=2.7.1.25 {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000256|RuleBase:RU004347};
DE AltName: Full=APS kinase {ECO:0000256|HAMAP-Rule:MF_00065};
DE AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00065};
DE AltName: Full=Adenosine-5'-phosphosulfate kinase {ECO:0000256|HAMAP-Rule:MF_00065};
GN Name=cysC {ECO:0000256|HAMAP-Rule:MF_00065};
GN ORFNames=A3C47_07340 {ECO:0000313|EMBL:OGW82857.1};
OS Omnitrophica bacterium RIFCSPHIGHO2_02_FULL_51_18.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1801823 {ECO:0000313|EMBL:OGW82857.1, ECO:0000313|Proteomes:UP000179119};
RN [1] {ECO:0000313|EMBL:OGW82857.1, ECO:0000313|Proteomes:UP000179119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000256|RuleBase:RU004347}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate
CC + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:456216; EC=2.7.1.25; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00065, ECO:0000256|RuleBase:RU004347};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 2/3. {ECO:0000256|HAMAP-Rule:MF_00065,
CC ECO:0000256|RuleBase:RU004347}.
CC -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000256|HAMAP-
CC Rule:MF_00065, ECO:0000256|RuleBase:RU004347}.
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:OGW82857.1}.
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DR EMBL; MHFI01000027; OGW82857.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1JQ77; -.
DR STRING; 1801823.A3C47_07340; -.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000179119; Unassembled WGS sequence.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR CDD; cd02027; APSK; 1.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00455; apsK; 1.
DR PANTHER; PTHR42700; SULFATE ADENYLYLTRANSFERASE; 1.
DR PANTHER; PTHR42700:SF1; SULFATE ADENYLYLTRANSFERASE; 1.
DR Pfam; PF01583; APS_kinase; 1.
DR Pfam; PF13328; HD_4; 1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00065,
KW ECO:0000256|RuleBase:RU004347};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000256|RuleBase:RU004347};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00065,
KW ECO:0000256|RuleBase:RU004347};
KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00065}.
FT DOMAIN 209..316
FT /note="HD/PDEase"
FT /evidence="ECO:0000259|SMART:SM00471"
FT ACT_SITE 89
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
FT BINDING 15..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
SQ SEQUENCE 371 AA; 41547 MW; BD20D9B20EB4B62C CRC64;
MNGDQPTGYT LWFTGLPCSG KTTLAQSVGQ ELAKIGYPVE YIDGDLIRKN LTKDLGFSKE
DRETNIGRAA FVASLLTKHG VMTLVSLVSP YRSMRENAKN LIGRFIEIHV SCPIEVCEKR
DTKGMYKLAC EGKIRNFTGV SDPFEEPSAP DLLVHSDKNS IGECTRQVID YLVGKGIVIP
PDPFPGNKFL TQVYRFAARA HRGQTRKGKN LPYIVHPLSV AKKLESLKYP EHVIAAGLLH
DALEDTGCEI EEIEKVAGKK AAKIVSEVTD PDKTVPWRRR KADYLAKLKK ASKEALAVSC
ADKIDNIESI IENVRQSGKK FTDQFSTGMK QKTQNYALIY KTIRARDPRC RLLDLYREKL
DKLGTLFQTI H
//
