ID A0A433HLU0_9BACI Unreviewed; 200 AA.
AC A0A433HLU0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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 ECO:0000313|EMBL:RUQ29361.1};
GN ORFNames=ELQ35_10385 {ECO:0000313|EMBL:RUQ29361.1};
OS Peribacillus cavernae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX NCBI_TaxID=1674310 {ECO:0000313|EMBL:RUQ29361.1, ECO:0000313|Proteomes:UP000267430};
RN [1] {ECO:0000313|EMBL:RUQ29361.1, ECO:0000313|Proteomes:UP000267430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L5 {ECO:0000313|EMBL:RUQ29361.1,
RC ECO:0000313|Proteomes:UP000267430};
RA Seuylemezian A., Vaishampayan P.;
RT "Bacillus chawlae sp. nov., Bacillus glennii sp. nov., and Bacillus saganii
RT sp. nov. Isolated from the Vehicle Assembly Building at Kennedy Space
RT Center where the Viking Spacecraft were Assembled.";
RL Submitted (DEC-2018) 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:RUQ29361.1}.
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DR EMBL; RYZZ01000010; RUQ29361.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A433HLU0; -.
DR OrthoDB; 9804504at2; -.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000267430; 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:UP000267430};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00065}.
FT ACT_SITE 111
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
SQ SEQUENCE 200 AA; 22492 MW; 6DFE93B3F5DAADE1 CRC64;
MSGIDPIDHI IWHKNTVSKD DKQKLNQHKS MMIWFTGLSG SGKSTLANAL EKVLHAQGIR
TYLLDGDNLR HGINKNLGFS LEDRQENIRR IAEVGKLFVD AGVIVLAAAI SPFEIDRKAA
RDLFEASEFI EVYVKCSLDE CEIRDPKGLY KKARAGEIKD FTGVSQPYEE PLSPELVLDT
STQSLDETLE QLFIFIKGRL
//
