ID A0A0P7I5C6_9RHOB Unreviewed; 691 AA.
AC A0A0P7I5C6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Adenylyl-sulfate kinase {ECO:0000256|HAMAP-Rule:MF_00065};
DE EC=2.7.1.25 {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 ORFNames=AKJ29_17800 {ECO:0000313|EMBL:KPN64464.1};
OS Aliiroseovarius crassostreae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Aliiroseovarius.
OX NCBI_TaxID=154981 {ECO:0000313|EMBL:KPN64464.1, ECO:0000313|Proteomes:UP000050471};
RN [1] {ECO:0000313|EMBL:KPN64464.1, ECO:0000313|Proteomes:UP000050471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CV919-312 {ECO:0000313|EMBL:KPN64464.1,
RC ECO:0000313|Proteomes:UP000050471};
RA Kessner L., Spinard E., Nelson D.;
RT "Draft genome sequence of Aliiroseovarius crassostreae CV919-312TSm, the
RT causative agent of Roseovarius Oyster Disease (formerly Juvenile Oyster
RT Disease).";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC {ECO:0000256|HAMAP-Rule:MF_00065}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate +
CC diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58243; EC=2.7.7.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000262};
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|HAMAP-Rule:MF_00065}.
CC -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000256|HAMAP-
CC Rule:MF_00065}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00065}.
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:KPN64464.1}.
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DR EMBL; LKBA01000004; KPN64464.1; -; Genomic_DNA.
DR RefSeq; WP_055188731.1; NZ_LKBA01000004.1.
DR AlphaFoldDB; A0A0P7I5C6; -.
DR STRING; 154981.AKJ29_17800; -.
DR OrthoDB; 9804504at2; -.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000050471; 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:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-EC.
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 CDD; cd00517; ATPS; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.10.400.10; Sulfate adenylyltransferase; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR025980; ATP-Sase_PUA-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR024951; Sulfurylase_cat_dom.
DR InterPro; IPR002650; Sulphate_adenylyltransferase.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR NCBIfam; TIGR00455; apsK; 1.
DR NCBIfam; TIGR00339; sopT; 1.
DR PANTHER; PTHR42700; SULFATE ADENYLYLTRANSFERASE; 1.
DR PANTHER; PTHR42700:SF1; SULFATE ADENYLYLTRANSFERASE; 1.
DR Pfam; PF01583; APS_kinase; 1.
DR Pfam; PF01747; ATP-sulfurylase; 1.
DR Pfam; PF14306; PUA_2; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00065}; Kinase {ECO:0000256|HAMAP-Rule:MF_00065};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00065};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:KPN64464.1};
KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065};
KW Reference proteome {ECO:0000313|Proteomes:UP000050471};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00065}.
FT DOMAIN 130..281
FT /note="ATP-sulfurylase PUA-like"
FT /evidence="ECO:0000259|Pfam:PF14306"
FT DOMAIN 292..506
FT /note="Sulphate adenylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01747"
FT BINDING 522..529
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
SQ SEQUENCE 691 AA; 77151 MW; E567E1C32D177E33 CRC64;
MPATPPPSSP TEDDLRFLLL RQLDAAPEGS QRAIAAAVGI SLGRLNGLLR ATADQGLIQI
GKRGGPDKRQ RFSYVITAKG AAEKTRLRDQ FLARKFAEYD ALHAELTGSS SGLSPLKHRT
HPMQDNLTPI PELYVSYESA QKLKVEAADL TSHDLSPRQI CDLELLMNGG FNPLKGFLSE
EDYNGVVENM RLADGTLWPM PITLDVSEEF ANSIELGQDI ALRDQEGVIL ATMTVTDRWE
PNKAREAEKV FGADDDAHPA VNYLHNVAGK IYLGGPIVGI QQPVHYDFRG RRDTPNELRA
YFRKLGWRRV VAFQTRNPLH RAHQELTFRA AREAQANLLI HPVVGMTKPG DIDHFTRVRC
YEAVLDQYPA ATTTMSLLNL AMRMAGPREA VWHGLIRKNH GCTHFIVGRD HAGPGKNSAG
EDFYGPYDAQ DLFREHEAEI GIEMVDFKHM VYVQDRAQYE PADEIEDKDN VTILNISGTE
LRRRLQEGLE IPEWFSFPTV VEELRKTKPP RAEQGFTVFF TGFSGSGKST IANALMVKLM
EMGGRPVTLL DGDIVRKNLS SELGFSKEHR DLNIRRIGYV ASEITKNGGI AICAPIAPYA
TTRRAVREDI EQFGAFVEVH VATSIEECER RDRKGLYKLA REGKIKEFTG ISDPYDVPVN
PELTVETENV EVDNCAHQVL LKLESMGLIK G
//
