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Database: UniProt
Entry: A0A177ZWJ2_9BACI
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ID   A0A177ZWJ2_9BACI        Unreviewed;       199 AA.
AC   A0A177ZWJ2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Adenylyl-sulfate kinase {ECO:0000256|ARBA:ARBA00012121, 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   ORFNames=ABB05_09205 {ECO:0000313|EMBL:OAK72204.1};
OS   Lederbergia galactosidilytica.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lederbergia.
OX   NCBI_TaxID=217031 {ECO:0000313|EMBL:OAK72204.1, ECO:0000313|Proteomes:UP000077881};
RN   [1] {ECO:0000313|EMBL:OAK72204.1, ECO:0000313|Proteomes:UP000077881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G25-74 {ECO:0000313|EMBL:OAK72204.1,
RC   ECO:0000313|Proteomes:UP000077881};
RA   Zheng Z., Sun M.;
RT   "Comparison of genome.";
RL   Submitted (MAY-2015) 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:OAK72204.1}.
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DR   EMBL; LDJR01000041; OAK72204.1; -; Genomic_DNA.
DR   RefSeq; WP_057989346.1; NZ_LDJR01000041.1.
DR   AlphaFoldDB; A0A177ZWJ2; -.
DR   STRING; 217031.ABB05_09205; -.
DR   PATRIC; fig|217031.6.peg.1948; -.
DR   OrthoDB; 9804504at2; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000077881; 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; BIFUNCTIONAL 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE SYNTHASE; 1.
DR   PANTHER; PTHR11055:SF1; PAPS SYNTHETASE, ISOFORM D; 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   Reference proteome {ECO:0000313|Proteomes:UP000077881};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00065}.
FT   ACT_SITE        104
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
SQ   SEQUENCE   199 AA;  22558 MW;  6B347002F38A5CC5 CRC64;
     MNIIWHESEV SKENRQKLKH HKSAIIWFTG LSGAGKSTIS SALEKELFSK SIHTYRLDGD
     NIRHGLNKDL GFKQEDRQEN IRRIGEVSKL LVDAGLLTLT AFISPYRTDR DLVRGMVETD
     EMIEVYVKAS LETCEARDPK GLYEKARRGE IKDFTGIDAP YEEPINPEIV LDTNNIGVKE
     SVAIIVEYLQ SNGYIGCEK
//
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