ID A0A1B1MJW3_STRLN Unreviewed; 178 AA.
AC A0A1B1MJW3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 ECO:0000313|EMBL:QMV10419.1};
GN ORFNames=GJU35_35335 {ECO:0000313|EMBL:QMV10419.1}, SLCG_1822
GN {ECO:0000313|EMBL:AXG52977.1}, SLINC_6593
GN {ECO:0000313|EMBL:ANS68817.1};
OS Streptomyces lincolnensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1915 {ECO:0000313|EMBL:ANS68817.1, ECO:0000313|Proteomes:UP000092598};
RN [1] {ECO:0000313|EMBL:ANS68817.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 2936 {ECO:0000313|EMBL:ANS68817.1};
RA Meng S.C.;
RT "Enhancement of antibiotic productionsby engineered nitrateutilization in
RT actinobacteria.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AXG52977.1, ECO:0000313|Proteomes:UP000253884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC-G {ECO:0000313|EMBL:AXG52977.1,
RC ECO:0000313|Proteomes:UP000253884};
RX PubMed=29574602; DOI=10.1007/s10295-018-2029-1;
RA Xu Y., Tan G., Ke M., Li J., Tang Y., Meng S., Niu J., Wang Y., Liu R.,
RA Wu H., Bai L., Zhang L., Zhang B.;
RT "Enhanced lincomycin production by co-overexpression of metK1 and metK2 in
RT Streptomyces lincolnensis.";
RL J. Ind. Microbiol. Biotechnol. 45:345-355(2018).
RN [3] {ECO:0000313|EMBL:QMV10419.1, ECO:0000313|Proteomes:UP000515335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B48 {ECO:0000313|EMBL:QMV10419.1,
RC ECO:0000313|Proteomes:UP000515335};
RX PubMed=32322696;
RA Wang R., Kong F., Wu H., Hou B., Kang Y., Cao Y., Duan S., Ye J., Zhang H.;
RT "Complete genome sequence of high-yield strain S. lincolnensis B48 and
RT identification of crucial mutations contributing to lincomycin
RT overproduction.";
RL Synth Syst Biotechnol 5:37-48(2020).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00065}.
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DR EMBL; CP016438; ANS68817.1; -; Genomic_DNA.
DR EMBL; CP022744; AXG52977.1; -; Genomic_DNA.
DR EMBL; CP046024; QMV10419.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B1MJW3; -.
DR STRING; 1915.SLINC_6593; -.
DR KEGG; sls:SLINC_6593; -.
DR PATRIC; fig|1915.4.peg.7274; -.
DR OrthoDB; 9804504at2; -.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000092598; Chromosome.
DR Proteomes; UP000253884; Chromosome.
DR Proteomes; UP000515335; Chromosome.
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; PTHR42700; SULFATE ADENYLYLTRANSFERASE; 1.
DR PANTHER; PTHR42700:SF1; SULFATE ADENYLYLTRANSFERASE; 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|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 Reference proteome {ECO:0000313|Proteomes:UP000092598};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00065}.
FT REGION 136..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
SQ SEQUENCE 178 AA; 19236 MW; 90508E8BCA1697C2 CRC64;
MTTGATVWLT GLPSAGKTTI AYELAGRLRE EGHLVEVLDG DEIREFISAG LGFSREDRHT
NVQRIGFVSE LLARNGVKVL VPVIAPYADS REAVRKRHQE GGTAYLEVHV ATPVEVCSVR
DVKGLYAKQA AGELSGLTGV DDPYEEPESP DLRIESQNQS VQESAASVYA LLSERGLA
//
