ID A0A357L9D7_9PROT Unreviewed; 633 AA. AC A0A357L9D7; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 03-AUG-2022, entry version 16. DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00062, ECO:0000256|HAMAP-Rule:MF_00065}; DE Includes: DE RecName: Full=Sulfate adenylyltransferase subunit 1 {ECO:0000256|HAMAP-Rule:MF_00062}; DE EC=2.7.7.4 {ECO:0000256|HAMAP-Rule:MF_00062}; DE AltName: Full=ATP-sulfurylase large subunit {ECO:0000256|HAMAP-Rule:MF_00062}; DE AltName: Full=Sulfate adenylate transferase {ECO:0000256|HAMAP-Rule:MF_00062}; DE Short=SAT {ECO:0000256|HAMAP-Rule:MF_00062}; DE Includes: 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=cysN {ECO:0000256|HAMAP-Rule:MF_00062}; GN Synonyms=cysC {ECO:0000256|HAMAP-Rule:MF_00065}; GN ORFNames=DEA50_01705 {ECO:0000313|EMBL:HBS33781.1}; OS Parvularcula sp. OC Bacteria; Proteobacteria; Alphaproteobacteria; Parvularculales; OC Parvularculaceae; Parvularcula; unclassified Parvularcula. OX NCBI_TaxID=1979207 {ECO:0000313|EMBL:HBS33781.1, ECO:0000313|Proteomes:UP000263803}; RN [1] {ECO:0000313|EMBL:HBS33781.1, ECO:0000313|Proteomes:UP000263803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UBA11151 {ECO:0000313|EMBL:HBS33781.1}; RX PubMed=30148503; DOI=.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny substantially RT revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). 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 -!- FUNCTION: Proposed to provide activated sulfate for transfer to Nod CC factor. ATP sulfurylase may be the GTPase, regulating ATP sulfurylase CC activity. {ECO:0000256|ARBA:ARBA00024872}. CC -!- FUNCTION: With CysD forms the ATP sulfurylase (ATPS) that catalyzes the CC adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and CC diphosphate, the first enzymatic step in sulfur assimilation pathway. CC APS synthesis involves the formation of a high-energy phosphoric- CC sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled CC to ATP hydrolysis by CysD. {ECO:0000256|HAMAP-Rule:MF_00062}. 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, ECO:0000256|HAMAP- CC Rule:MF_00062}; 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 1/3. {ECO:0000256|HAMAP-Rule:MF_00062}. CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from CC sulfate: step 2/3. {ECO:0000256|HAMAP-Rule:MF_00065}. CC -!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and CysN. CC {ECO:0000256|HAMAP-Rule:MF_00062}. CC -!- SUBUNIT: Sulfate-activating enzymes, NodP and NodQ, may be physically CC associated. {ECO:0000256|ARBA:ARBA00011760}. CC -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000256|HAMAP- CC Rule:MF_00065}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. CysN/NodQ CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00062}. 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:HBS33781.1}. 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; DOIY01000037; HBS33781.1; -; Genomic_DNA. DR EnsemblBacteria; HBS33781; HBS33781; DEA50_01705. DR UniPathway; UPA00140; UER00204. DR Proteomes; UP000263803; 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-UniRule. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-UniRule. 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; cd04166; CysN_ATPS; 1. DR CDD; cd03695; CysN_NodQ_II; 1. DR CDD; cd04095; CysN_NoDQ_III; 1. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 1. DR HAMAP; MF_00062; Sulf_adenylyltr_sub1; 1. DR InterPro; IPR002891; APS_kinase. DR InterPro; IPR041757; CysN_GTP-bd. DR InterPro; IPR044138; CysN_II. DR InterPro; IPR044139; CysN_NoDQ_III. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR011779; SO4_adenylTrfase_lsu. 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 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; TIGR02034; CysN; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00062}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_00062}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000313|EMBL:HBS33781.1}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00062}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP- KW Rule:MF_00062}; Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00062}. FT DOMAIN 22..237 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" FT ACT_SITE 541 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065" FT BINDING 31..38 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00062" FT BINDING 110..114 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00062" FT BINDING 165..168 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00062" FT BINDING 467..474 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065" SQ SEQUENCE 633 AA; 69854 MW; AA724A82CA13973B CRC64; MTHAAALAAD DVLAYLDAHE KKSMLRFITC GSVDDGKSTL IGRLLYDTKL LYEDQLAALE ADSKKVGTQG DKIDFALLVD GLAAEREQGI TIDVAYRFFS TEKRKFIVAD TPGHEQYTRN MATGASTADV AVILIDARQG VLKQTRRHSF IASLLGIRHI VVAVNKMDIV GYSEAVFDRI EADYRAFAGK LSFESIVAIP MSALEGDNIT TKSANTRWFN GPALLPYLET IEVESGREDL PFRLPVQWVN RPNLDFRGFS GTIASGAVKP GDEVVVIPSG RRSSVKRIVT QDGDLPAAGP HRAVTLTLAD EIDISRGDIL CAAKAPAEQS DQFAAHIIWM HDEEMIPGRQ YFFKTANRVV SGSITELKHK INVNTLEHMS GKTLELNEVG VCNVSTSAPI AFDPYRENRE TGSFIIIDKR TNNTVGVGMI DFSLRRAQNV HWQDLDVNKV ARARAKHQRP CVLWFTGLSG AGKSTVANLV EKRLHDMGRH TYTLDGDNVR HGLNKDLGFT DADRVENIRR VSETAKLMVD AGLIVLVSFI SPFQSERRMA REALEDGEFI EIFVSTPLAV CEKRDVKGLY AKARRGEIRN FTGIDSDYEA PENPELTLDT SKVTAADAAT AIVEHLRKNG YLG //