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Database: UniProt
Entry: A0A2A5CU38_9GAMM
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ID   A0A2A5CU38_9GAMM        Unreviewed;       205 AA.
AC   A0A2A5CU38;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Adenylyl-sulfate kinase {ECO:0000256|ARBA:ARBA00018163, ECO:0000256|HAMAP-Rule:MF_00065};
DE            EC=2.7.1.25 {ECO:0000256|ARBA:ARBA00012121, ECO:0000256|HAMAP-Rule:MF_00065};
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   ECO:0000313|EMBL:PCJ47055.1};
GN   ORFNames=COA99_01645 {ECO:0000313|EMBL:PCJ47055.1};
OS   Moraxellaceae bacterium.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae.
OX   NCBI_TaxID=1889775 {ECO:0000313|EMBL:PCJ47055.1, ECO:0000313|Proteomes:UP000218379};
RN   [1] {ECO:0000313|Proteomes:UP000218379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy inhabits the
RT   cold, oxic subseafloor aquifer.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC       {ECO:0000256|ARBA:ARBA00002632, ECO:0000256|HAMAP-Rule:MF_00065,
CC       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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001823, 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|ARBA:ARBA00004806, ECO:0000256|HAMAP-
CC       Rule:MF_00065, ECO:0000256|RuleBase:RU004347}.
CC   -!- SIMILARITY: Belongs to the APS kinase family.
CC       {ECO:0000256|ARBA:ARBA00007008, ECO:0000256|HAMAP-Rule:MF_00065,
CC       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:PCJ47055.1}.
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DR   EMBL; NVVG01000007; PCJ47055.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A5CU38; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000218379; 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   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; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00455; apsK; 1.
DR   PANTHER; PTHR11055:SF1; 3'-PHOSPHOADENOSINE-5'-PHOSPHOSULFATE SYNTHASE; 1.
DR   PANTHER; PTHR11055; BIFUNCTIONAL 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE SYNTHASE; 1.
DR   Pfam; PF01583; APS_kinase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00065};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000256|RuleBase:RU004347};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00065}; Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00065}.
FT   ACT_SITE        110
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
FT   BINDING         36..43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
SQ   SEQUENCE   205 AA;  22906 MW;  62322EC1D0AC272E CRC64;
     MTDQKATNVH WHDGDVSHQD RQDLLGQKGV TLWFTGLSGS GKSTIAVALE KALIKRGKLA
     YRLDGDNIRM GINKNLGFTA EDRTENIRRI GEISKLFVDA GTIVLSSFIS PYTADRDQAR
     KIHTESGFPF IEIFVDCALE EAEKRDPKGL YKKARAGEIK GFTGIDDPYE APANPEIHLR
     TDQMTLDEEV NLLIDELVKQ GFLID
//
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