UniProt: A0A0C1YF49

Database: UniProt
Entry: A0A0C1YF49_9CYAN

LinkDB:  A0A0C1YF49_9CYAN 
Original site:  A0A0C1YF49_9CYAN

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (3)   
   InterPro (2)   
   Pfam (1)   
Literature (1)   
   PubMed (1)   
All databases (11)   

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ID   A0A0C1YF49_9CYAN        Unreviewed;       181 AA.
AC   A0A0C1YF49;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
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:NEV67209.1};
GN   ORFNames=QQ91_008765 {ECO:0000313|EMBL:NEV67209.1};
OS   Lyngbya confervoides BDU141951.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Lyngbya.
OX   NCBI_TaxID=1574623 {ECO:0000313|EMBL:NEV67209.1, ECO:0000313|Proteomes:UP000031561};
RN   [1] {ECO:0000313|EMBL:NEV67209.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BDU141951 {ECO:0000313|EMBL:NEV67209.1};
RA   Malar M.C., Sen D., Tripathy S.;
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:NEV67209.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BDU141951 {ECO:0000313|EMBL:NEV67209.1};
RX   PubMed=25745003;
RA   Chandrababunaidu M.M., Sen D., Tripathy S.;
RT   "Draft Genome Sequence of Filamentous Marine Cyanobacterium Lyngbya
RT   confervoides Strain BDU141951.";
RL   Genome Announc. 3:e00066-e00015(2015).
RN   [3] {ECO:0000313|EMBL:NEV67209.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BDU141951 {ECO:0000313|EMBL:NEV67209.1};
RA   Sarangi A.N., Ghosh S., Mukherjee M., Tripathy S.;
RL   Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
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: 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:NEV67209.1}.
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DR   EMBL; JTHE02000003; NEV67209.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C1YF49; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000031561; 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; 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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00065}.
FT   ACT_SITE        86
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
FT   BINDING         12..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
SQ   SEQUENCE   181 AA;  20002 MW;  10EA5C3256D46247 CRC64;
     MEHRGVTVWL TGLSGAGKST ITEALAQRLR DRQCKLEVLD GDIVRTNLTK GLGFSKEDRD
     TNIRRIGFVS HLLTRNGVIV LVSAISPYRA VREEVRATIG DFMEVYVSAP LEVCESRDVK
     GLYKKARAGE IKQFTGIDDP YEPPANPEVN CETHKESLDE SVDKVIAKLE EMGYLPAGVP
     A
//

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