ID A0A1F8NZ26_9CHLR Unreviewed; 579 AA.
AC A0A1F8NZ26;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=A2Y93_02995 {ECO:0000313|EMBL:OGO16109.1};
OS Chloroflexi bacterium RBG_13_68_17.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797638 {ECO:0000313|EMBL:OGO16109.1, ECO:0000313|Proteomes:UP000178211};
RN [1] {ECO:0000313|EMBL:OGO16109.1, ECO:0000313|Proteomes:UP000178211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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; Evidence={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: 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:OGO16109.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MGNF01000019; OGO16109.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8NZ26; -.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000178211; 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 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 NCBIfam; TIGR00455; apsK; 1.
DR NCBIfam; TIGR00339; sopT; 1.
DR PANTHER; PTHR42700:SF3; BIFUNCTIONAL SAT_APS KINASE-RELATED; 1.
DR PANTHER; PTHR42700; 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.
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:OGO16109.1};
KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00065}.
FT DOMAIN 10..165
FT /note="ATP-sulfurylase PUA-like"
FT /evidence="ECO:0000259|Pfam:PF14306"
FT DOMAIN 174..390
FT /note="Sulphate adenylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01747"
FT ACT_SITE 480
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
FT BINDING 406..413
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
SQ SEQUENCE 579 AA; 65155 MW; E85E5D6C812C8007 CRC64;
MNAVSTSTLI EPYGGRLVDL TIPEQALEET KARASTMLSI GLTERSVCDL ELLATGAFSP
LDRFMGEASY GRVIEEMRLE DGHIFPIPIT LPYDGKDPIQ LDQEIVLRDQ KNEILAIMRL
EEIYPWDRRA AASRVFGTTD LRHPLVAEMQ RWGSHFISGP LQVVQLPPHY DYKELRLTPA
DTRARLETYN RRHVVAFQTR NPLHRAHEEL TKRAIEEVDG VLLLHPVVGM TKPGDVDHFT
RVRTYRALAS RYYDPQRVLL ALLPLAMRLA GPREALWHAV IRRNHGANHL IVGRDHASPG
SDSTGKPFYG PYDAQELVAR YSAELGVKMI PFRELVYLPQ HDRFEETTKI PEGALQASIS
GTQVREEYLN NGTRLPGWFT RPEVAEILAE AYPPRHKRGV CIWFTGLSGA GKSTTAEVLT
VLLQERGRQV TVLDGDVVRT HLSKGLGFNR EDRDINIRRI GYVASEIVRH GGVTICSAIS
PYRAARNDVR AMVGSDQFVE VFVDTPVEVC EARDKKGLYA KARRGEIRGF TGIDDPYEAP
EKPEMVLETL EHSPEENARM ILEHLRGMGI LRSDPAVGD
//
