ID J2SIS1_FLASC Unreviewed; 177 AA.
AC J2SIS1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Adenylyl-sulfate kinase {ECO:0000256|RuleBase:RU004347};
DE EC=2.7.1.25 {ECO:0000256|RuleBase:RU004347};
GN ORFNames=PMI10_01253 {ECO:0000313|EMBL:EJL65357.1};
OS Flavobacterium sp. (strain CF136).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1144313 {ECO:0000313|EMBL:EJL65357.1, ECO:0000313|Proteomes:UP000007287};
RN [1] {ECO:0000313|EMBL:EJL65357.1, ECO:0000313|Proteomes:UP000007287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF136 {ECO:0000313|EMBL:EJL65357.1,
RC ECO:0000313|Proteomes:UP000007287};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
CC -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
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|RuleBase:RU004347};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 2/3. {ECO:0000256|RuleBase:RU004347}.
CC -!- SIMILARITY: Belongs to the APS kinase family.
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:EJL65357.1}.
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DR EMBL; AKJZ01000015; EJL65357.1; -; Genomic_DNA.
DR RefSeq; WP_007805720.1; NZ_AKJZ01000015.1.
DR AlphaFoldDB; J2SIS1; -.
DR STRING; 1144313.PMI10_01253; -.
DR PATRIC; fig|1144313.4.peg.1251; -.
DR eggNOG; COG0529; Bacteria.
DR OrthoDB; 9804504at2; -.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000007287; Unassembled WGS sequence.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:InterPro.
DR CDD; cd02027; APSK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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|RuleBase:RU004347};
KW Kinase {ECO:0000256|RuleBase:RU004347, ECO:0000313|EMBL:EJL65357.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU004347};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004347}.
SQ SEQUENCE 177 AA; 20186 MW; F6FE7870ADFAAF3C CRC64;
MILIQFTGLS GSGKTTLAKN VEHLLVEKGH KVEIVDGDIY RKTLCKDLGF SKDDRCENVR
RLFNVGQDFV QSEVIVLMSV INPYEDLRNE IRQYDFVRTV FLDCSIDNLI KRDPKGLYQK
ALLPDNDSNK IKNFTGISDV YEVPLKADLT LKTDSEPESV STNKLYYFII DNITNAV
//
