ID A3NWW3_BURP0 Unreviewed; 489 AA.
AC A3NWW3;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
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|ARBA:ARBA00031393, ECO:0000256|HAMAP-Rule:MF_00065};
DE AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase {ECO:0000256|ARBA:ARBA00031464, ECO:0000256|HAMAP-Rule:MF_00065};
DE AltName: Full=Adenosine-5'-phosphosulfate kinase {ECO:0000256|ARBA:ARBA00029724, ECO:0000256|HAMAP-Rule:MF_00065};
GN Name=cysC {ECO:0000256|HAMAP-Rule:MF_00065,
GN ECO:0000313|EMBL:ABN88896.1};
GN OrderedLocusNames=BURPS1106A_2580 {ECO:0000313|EMBL:ABN88896.1};
OS Burkholderia pseudomallei (strain 1106a).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=357348 {ECO:0000313|EMBL:ABN88896.1, ECO:0000313|Proteomes:UP000006738};
RN [1] {ECO:0000313|EMBL:ABN88896.1, ECO:0000313|Proteomes:UP000006738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1106a {ECO:0000313|EMBL:ABN88896.1,
RC ECO:0000313|Proteomes:UP000006738};
RA DeShazer D., Woods D.E., Nierman W.C.;
RL Submitted (FEB-2007) 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 -!- 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};
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}.
CC -!- SIMILARITY: Belongs to the APS kinase family.
CC {ECO:0000256|ARBA:ARBA00007008, ECO:0000256|HAMAP-Rule:MF_00065}.
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DR EMBL; CP000572; ABN88896.1; -; Genomic_DNA.
DR AlphaFoldDB; A3NWW3; -.
DR KEGG; bpl:BURPS1106A_2580; -.
DR HOGENOM; CLU_041890_0_0_4; -.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000006738; Chromosome I.
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; cd02440; AdoMet_MTases; 1.
DR CDD; cd02027; APSK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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:0000313|EMBL:ABN88896.1};
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 387
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
FT BINDING 313..320
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
SQ SEQUENCE 489 AA; 51418 MW; F6C59DF1F665E614 CRC64;
MRSCDDFLRT SELSIAAVNS LRRTIAPSHR VLDACGSGAA CLLASRYGAK QVVALAAAEA
TLVGARAGAN GPGERISFVD AEQAAALVAR QGRFDVVLGL AGGGRDGLDP HYGARLDAFA
RRFGTANVAV VPNGVRYDAQ LVEWREAERL EADVAARQRA LEARYDLTLG PVLDQVAAGA
APRGRVRADA LRALCARLPF LSCRPGDGGD AGTSGTSGTA APEHVELTAA HGGRADGVLW
TQELIHDGIV IERIQGCSWL DERVDLEAGD AIAVPVADMA RAAPLDGGEA PPQLAPAPRA
SGAPAPLVFW LTGISGAGKT TIATRFKQRA DADAWPTVVL DGDTLRGGLN ADLGFCDADR
AENVRRIAEV AALMADTGLV VVVSCISPRR SFRETAREIV GAERFVEVFV DTPPAVAQAR
DPKGLYRRAR AGLIASFTGI DSDYEPPPDP QLRIDTTTHD VEDATQMLRR YYVDARLSGA
RAGTAECAA
//
