ID A0A4Y8P9A4_9BACT Unreviewed; 636 AA. AC A0A4Y8P9A4; DT 18-SEP-2019, integrated into UniProtKB/TrEMBL. DT 18-SEP-2019, sequence version 1. DT 24-JAN-2024, entry version 18. 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=A7Q10_09825 {ECO:0000313|EMBL:TFE67211.1}; OS Methylacidiphilum caldifontis. OC Bacteria; Verrucomicrobiota; Methylacidiphilae; Methylacidiphilales; OC Methylacidiphilaceae; Methylacidiphilum (ex Ratnadevi et al. 2023). OX NCBI_TaxID=2795386 {ECO:0000313|EMBL:TFE67211.1, ECO:0000313|Proteomes:UP000297713}; RN [1] {ECO:0000313|EMBL:TFE67211.1, ECO:0000313|Proteomes:UP000297713} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Phi {ECO:0000313|EMBL:TFE67211.1, RC ECO:0000313|Proteomes:UP000297713}; RA Erikstad H.-A., Smestad N.B., Ceballos R.M., Birkeland N.-K.; RT "Diversity and Homogeneity among Thermoacidophilic Verrucomicrobia RT Methanotrophs Linked with Geographical Origin."; RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: APS kinase catalyzes the synthesis of activated sulfate. CC {ECO:0000256|ARBA:ARBA00002357}. 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 -!- SIMILARITY: In the C-terminal section; belongs to the APS kinase CC family. {ECO:0000256|ARBA:ARBA00005438}. CC -!- SIMILARITY: In the N-terminal section; belongs to the TRAFAC class CC translation factor GTPase superfamily. Classic translation factor CC GTPase family. CysN/NodQ subfamily. {ECO:0000256|ARBA:ARBA00007237}. 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:TFE67211.1}. 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; LXQC01000158; TFE67211.1; -; Genomic_DNA. DR AlphaFoldDB; A0A4Y8P9A4; -. DR OrthoDB; 9804504at2; -. DR UniPathway; UPA00140; UER00205. DR Proteomes; UP000297713; 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:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:RHEA. 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; cd04095; CysN_NoDQ_III; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR Gene3D; 2.40.30.10; Translation factors; 2. DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 1. DR InterPro; IPR002891; APS_kinase. DR InterPro; IPR044139; CysN_NoDQ_III. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; T_Tr_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel_sf. DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C. DR NCBIfam; TIGR00455; apsK; 1. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR23115:SF170; ELONGATION FACTOR 1-ALPHA 2; 1. DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1. DR Pfam; PF01583; APS_kinase; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR SUPFAM; SSF50447; Translation proteins; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00065}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000313|EMBL:TFE67211.1}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00065}; Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00065}. FT DOMAIN 9..220 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" FT ACT_SITE 527 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065" FT BINDING 453..460 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065" SQ SEQUENCE 636 AA; 70559 MW; 5F630C6D152B8A01 CRC64; MKNLLPLEAK SLNVIFAGHV DHGKSTLIGR ILWETDAISK EKKETAIAYC KKNNIAFEYA FLLDSLVEER TQNITIDVTE VHFFYGQRRF RIIDAPGHLE FLKNMISGAA KADCAVLVID ASSGIGDQTK RHAMLLSLLG INQIVIALNK FDLVHYSQHS YETLSQECKS LFERLGLSYL SIVPLSAKAG ENIVERSSRL SWYRGGSLLE VLLGLKSSAS AESSPLRLPI QDIYRFDDRR LLAGRVEAGK IEQGDLICFF PSGKKSRVKA IHHWPAESSP RLVTAGKSTA IQLEDEIFVE RGEIIAHENS APLVATDFSA RLFWLGDLPL VIGAPYIFRL ATGQCMARVL QINRVIDGST LEDLKPIPIE VKKNETAEII LRTSAPIACD PFDQIQSTGR FVLADKDRIS GGGIILKALP SKPLHETQSL SRISSIQRIK FLGHRSGVFW MTGLSGSGKT TLSNRLEQML FHRGILAYVI DGDELRSGLS KDLGFDAQDR RENIRRAAEL AKTLAKSGLV VIVALISPFD ADRKNARAIC EKQGVLFKEI YIDAPLEVCK ARDPKFLYLK ASKGEIPKMT GLDSPYEPPQ QCDLHLLTAE ESIESCLGKL LDFIIPLVRI SPDKEKELLE DPAAEI //