ID A0A357L9D7_9PROT Unreviewed; 633 AA. AC A0A357L9D7; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 10-APR-2019, entry version 5. 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. OX NCBI_TaxID=1979207 {ECO:0000313|EMBL:HBS33781.1}; RN [1] {ECO:0000313|EMBL:HBS33781.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UBA11151 {ECO:0000313|EMBL:HBS33781.1}; RX PubMed=30148503; DOI=10.1038/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 RT substantially revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). 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:SAAS01122058}; 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 1/3. {ECO:0000256|HAMAP-Rule:MF_00062}. CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite CC from sulfate: step 2/3. {ECO:0000256|HAMAP-Rule:MF_00065}. CC -!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and CC CysN. {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 -!- 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: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 UniPathway; UPA00140; UER00204. 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 HAMAP; MF_00065; Adenylyl_sulf_kinase; 1. DR HAMAP; MF_00062; Sulf_adenylyltr_sub1; 1. DR InterPro; IPR002891; APS_kinase. 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; 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 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|HAMAP-Rule:MF_00062, KW ECO:0000256|SAAS:SAAS00444459}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00062, KW ECO:0000256|SAAS:SAAS00055993}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00065, KW ECO:0000256|SAAS:SAAS01092249, ECO:0000313|EMBL:HBS33781.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00062, KW ECO:0000256|SAAS:SAAS00055970}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00062, KW ECO:0000256|SAAS:SAAS00056011, ECO:0000313|EMBL:HBS33781.1}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00062, KW ECO:0000256|SAAS:SAAS00056018, ECO:0000313|EMBL:HBS33781.1}. FT DOMAIN 22 237 Tr-type G. {ECO:0000259|PROSITE:PS51722}. FT NP_BIND 31 38 GTP. {ECO:0000256|HAMAP-Rule:MF_00062}. FT NP_BIND 110 114 GTP. {ECO:0000256|HAMAP-Rule:MF_00062}. FT NP_BIND 165 168 GTP. {ECO:0000256|HAMAP-Rule:MF_00062}. FT NP_BIND 467 474 ATP. {ECO:0000256|HAMAP-Rule:MF_00065}. FT ACT_SITE 541 541 Phosphoserine intermediate. FT {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 //