ID A0A4P6V0K4_9HYPH Unreviewed; 639 AA. AC A0A4P6V0K4; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 24-JUL-2024, entry version 21. 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 ECO:0000313|EMBL:QBK30046.1}; GN Synonyms=cysC {ECO:0000256|HAMAP-Rule:MF_00065}; GN ORFNames=E0E05_05195 {ECO:0000313|EMBL:QBK30046.1}; OS Roseitalea porphyridii. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Phyllobacteriaceae; Roseitalea. OX NCBI_TaxID=1852022 {ECO:0000313|EMBL:QBK30046.1, ECO:0000313|Proteomes:UP000293719}; RN [1] {ECO:0000313|EMBL:QBK30046.1, ECO:0000313|Proteomes:UP000293719} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MA7-20 {ECO:0000313|EMBL:QBK30046.1, RC ECO:0000313|Proteomes:UP000293719}; RX PubMed=27902230; DOI=.1099/ijsem.0.001633; RA Hyeon J.W., Jeong S.E., Baek K., Jeon C.O.; RT "Roseitalea porphyridii gen. nov., sp. nov., isolated from a red alga, and RT reclassification of Hoeflea suaedae Chung et al. 2013 as Pseudohoeflea RT suaedae gen. nov., comb. nov."; RL Int. J. Syst. Evol. Microbiol. 67:362-368(2017). 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 --------------------------------------------------------------------------- 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; CP036532; QBK30046.1; -; Genomic_DNA. DR AlphaFoldDB; A0A4P6V0K4; -. DR KEGG; rpod:E0E05_05195; -. DR OrthoDB; 9804504at2; -. DR UniPathway; UPA00140; UER00204. DR Proteomes; UP000293719; Chromosome. 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:0003746; F:translation elongation factor activity; IEA:TreeGrafter. DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway. 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; 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 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; IPR011779; SO4_adenylTrfase_lsu. DR InterPro; IPR000795; T_Tr_GTP-bd_dom. DR InterPro; IPR050100; TRAFAC_GTPase_members. DR InterPro; IPR009000; Transl_B-barrel_sf. DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C. DR NCBIfam; TIGR00455; apsK; 1. DR NCBIfam; TIGR02034; CysN; 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; 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}; Kinase {ECO:0000256|HAMAP-Rule:MF_00065}; 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 Reference proteome {ECO:0000313|Proteomes:UP000293719}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00062}. FT DOMAIN 23..239 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" FT ACT_SITE 543 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065" FT BINDING 32..39 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00062" FT BINDING 111..115 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00062" FT BINDING 166..169 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00062" FT BINDING 469..476 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065" SQ SEQUENCE 639 AA; 69495 MW; 8F12B6AEB1F706A4 CRC64; MAHHVSDLAA SDIAAYLAAH EEKSLLRFLT CGSVDDGKST LIGRLLYESK LVFEDQLDAL YNDSRRLGTQ GNRPDLALLV DGLASEREQG ITIDVAYRFF STEKRKFIVA DTPGHEQYTR NMATGASTAD LAIILVDARK GILTQTRRHS FIVSRLGIRN IVVAVNKMDL VDYDPAVFRR IEREYALLAR ALGEDLDITA IPISALEGDN VIAPSAAMPW YDGPTLMEHL EQVEVEDARA AAPFRLPVQW VNRPDLDFRG FAGQIAGGSV RVGDPVTVLP SGLTSTVTGI VTMDEQRAEA IAGQSVTLTL AHEIDVSRGD MLVASEAPAQ TGDRFEATIL WMADEKMFPG RSYWIKTAGG TAQATIGAPD HRVDINTLAT EPARNLALNE IGVCAVTLDR PIAFDAYADN RDTGSFILID RLTNATVGMG MIHRALSRSA NIHWQATEID RQARAALKGH RPAVVWFTGL SGSGKSTIAN LVEARLAAAQ VHTMLLDGDN VRHGLNRDLG FSDTDRVENI RRIAEVARLM TEAGLVTLVS FISPFRAERR MARSLVPDGE FFLVHVDTPL KVAEARDPKG LYAKARAGEI ANFTGIGSPY ERPEQPDLRI DTTALTAQEA ADLVIAELAR RGIIAAAGI //