ID A0A4Y8P9A4_9BACT Unreviewed; 636 AA. AC A0A4Y8P9A4; DT 18-SEP-2019, integrated into UniProtKB/TrEMBL. DT 18-SEP-2019, sequence version 1. DT 13-NOV-2019, entry version 3. 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 sp. Phi. OC Bacteria; Verrucomicrobia; Methylacidiphilae; Methylacidiphilales; OC Methylacidiphilaceae; Methylacidiphilum; OC unclassified Methylacidiphilum. OX NCBI_TaxID=1847729 {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: Catalyzes the synthesis of activated sulfate. CC {ECO:0000256|HAMAP-Rule:MF_00065}. CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl CC sulfate + 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 CC from 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 CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule. DR CDD; cd02027; APSK; 1. DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 1. DR InterPro; IPR002891; APS_kinase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; TF_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel_sf. DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C. DR Pfam; PF00009; GTP_EFTU; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF50465; SSF50465; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR00455; apsK; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00065}; KW Complete proteome {ECO:0000313|Proteomes:UP000297713}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00065, KW ECO:0000256|SAAS:SAAS01092249, ECO:0000313|EMBL:TFE67211.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00065}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00065}. FT DOMAIN 9 220 Tr-type G. {ECO:0000259|PROSITE:PS51722}. FT NP_BIND 453 460 ATP. {ECO:0000256|HAMAP-Rule:MF_00065}. FT ACT_SITE 527 527 Phosphoserine intermediate. FT {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 //