ID A0A4P6V0K4_9RHIZ Unreviewed; 639 AA. AC A0A4P6V0K4; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 11-DEC-2019, entry version 4. 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; Proteobacteria; Alphaproteobacteria; Rhizobiales; 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: Catalyzes the synthesis of activated sulfate. CC {ECO:0000256|HAMAP-Rule:MF_00065}. CC -!- FUNCTION: May be the GTPase, regulating ATP sulfurylase activity. CC {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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00062, ECO:0000256|SAAS:SAAS01159104}; 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 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 -!- 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 --------------------------------------------------------------------------- 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 KEGG; rpod:E0E05_05195; -. DR KO; K00955; -. 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: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 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; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011779; SO4_adenylTrfase_lsu. 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; TIGR02034; CysN; 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|HAMAP-Rule:MF_00062, KW ECO:0000256|SAAS:SAAS01159110}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00062, KW ECO:0000256|SAAS:SAAS01159120}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000256|SAAS:SAAS01092249}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00062, KW ECO:0000256|SAAS:SAAS01159098}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00062, KW ECO:0000256|SAAS:SAAS01159099, ECO:0000313|EMBL:QBK30046.1}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00062, KW ECO:0000256|SAAS:SAAS01159119, ECO:0000313|EMBL:QBK30046.1}. FT DOMAIN 23..239 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" FT NP_BIND 32..39 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00062" FT NP_BIND 111..115 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00062" FT NP_BIND 166..169 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00062" FT NP_BIND 469..476 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065" FT ACT_SITE 543 FT /note="Phosphoserine intermediate" 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 //