ID A0A1M7P524_9PSED Unreviewed; 632 AA. AC A0A1M7P524; DT 15-MAR-2017, integrated into UniProtKB/TrEMBL. DT 15-MAR-2017, sequence version 1. DT 02-JUN-2021, entry version 16. 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}; GN Name=cysN {ECO:0000256|HAMAP-Rule:MF_00062}; GN ORFNames=SAMN05216593_10896 {ECO:0000313|EMBL:SHN11664.1}; OS Pseudomonas asturiensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1190415 {ECO:0000313|EMBL:SHN11664.1, ECO:0000313|Proteomes:UP000183983}; RN [1] {ECO:0000313|EMBL:SHN11664.1, ECO:0000313|Proteomes:UP000183983} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 26898 {ECO:0000313|EMBL:SHN11664.1, RC ECO:0000313|Proteomes:UP000183983}; RA Jaros S., Januszkiewicz K., Wedrychowicz H.; RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: APS kinase catalyzes the synthesis of activated sulfate. CC {ECO:0000256|ARBA:ARBA00002357}. 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; CC Evidence={ECO:0000256|ARBA:ARBA00000262, ECO:0000256|HAMAP- CC Rule:MF_00062}; 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|ARBA:ARBA00004806}. CC -!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and CysN. CC {ECO:0000256|HAMAP-Rule:MF_00062}. 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; FRDA01000008; SHN11664.1; -; Genomic_DNA. DR RefSeq; WP_073168329.1; NZ_FRDA01000008.1. DR EnsemblBacteria; SHN11664; SHN11664; SAMN05216593_10896. DR UniPathway; UPA00140; UER00204. DR Proteomes; UP000183983; Unassembled WGS sequence. DR GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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 CDD; cd03695; CysN_NodQ_II; 1. DR CDD; cd04095; CysN_NoDQ_III; 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; 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}; Kinase {ECO:0000313|EMBL:SHN11664.1}; 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}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00062}. FT DOMAIN 22..241 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" FT NP_BIND 31..38 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00062" FT NP_BIND 110..114 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00062" FT NP_BIND 165..168 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00062" SQ SEQUENCE 632 AA; 69029 MW; BE0B773EAF1CB665 CRC64; MSHQSDLISE DILAYLGQHE RKEMLRFLTC GNVDDGKSTL IGRLLHDSKM IYEDHLEAIT RDSKKSGTTG DDVDLALLVD GLQAEREQGI TIDVAYRYFS TAKRKFIIAD TPGHEQYTRN MATGASTCDL AIILVDARYG VQTQTRRHSY IASLLGIKHI VVAINKMDLN GFDESVFESI KADYLKFADG IAFKPTTMAF VPMSALKGDN VVNRSERSPW YTGQSLMEIL ETVEIASDRN YTDLRFPVQY VNRPNLNFRG FAGTLASGIV HKGDEIVVLP SGKSSRVKSI VTFEGELEQA GPGQAVTLTM EDEIDISRGD LLVHADNVPQ VSDAFDAMLV WMAEEPMLPG KKYDIKRATS YVPGSIASIT HRVDVNTLVE GPASSLQLNE IGRVKISLDA PIALDGYDSN RTTGAFIVID RLTNGTVAAG MIIAKPVNAG GATHHGDLAH VTTQERAQRF GQQPATVLFS GLSGAGKSTL AYAVERKLFD MGRAVYVLDG QNLRHDLNKG LPQNRAGRTE NWSRAAHVAR QFNEAGLLTL AAFVAPDAEG RERVKALIGK ERLVTVYVQA SPAVCRERDP QGLYAADGDN IPGESFPYDV PLDADLVIDT QALTVDEGVK LVLDMLRSRG AI //