ID A0A0H3AS38_BRUO2 Unreviewed; 644 AA. AC A0A0H3AS38; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 27-NOV-2024, entry version 51. 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=cysNC {ECO:0000313|EMBL:ABQ61198.1}; GN Synonyms=cysC {ECO:0000256|HAMAP-Rule:MF_00065}, cysN GN {ECO:0000256|HAMAP-Rule:MF_00062}; GN OrderedLocusNames=BOV_0186 {ECO:0000313|EMBL:ABQ61198.1}; OS Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=444178 {ECO:0000313|EMBL:ABQ61198.1, ECO:0000313|Proteomes:UP000006383}; RN [1] {ECO:0000313|Proteomes:UP000006383} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25840 / 63/290 / NCTC 10512 RC {ECO:0000313|Proteomes:UP000006383}; RX PubMed=19436743; DOI=10.1371/journal.pone.0005519; RA Tsolis R.M., Seshadri R., Santos R.L., Sangari F.J., Lobo J.M., RA de Jong M.F., Ren Q., Myers G., Brinkac L.M., Nelson W.C., Deboy R.T., RA Angiuoli S., Khouri H., Dimitrov G., Robinson J.R., Mulligan S., RA Walker R.L., Elzer P.E., Hassan K.A., Paulsen I.T.; RT "Genome degradation in Brucella ovis corresponds with narrowing of its host RT range and tissue tropism."; RL PLoS ONE 4:E5519-E5519(2009). 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=sulfate + ATP + H(+) = 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; CP000708; ABQ61198.1; -; Genomic_DNA. DR RefSeq; WP_005977860.1; NC_009505.1. DR AlphaFoldDB; A0A0H3AS38; -. DR GeneID; 45123679; -. DR KEGG; bov:BOV_0186; -. DR HOGENOM; CLU_007265_5_0_5; -. DR UniPathway; UPA00140; UER00204. DR Proteomes; UP000006383; Chromosome I. 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 FunFam; 3.40.50.300:FF:000119; Sulfate adenylyltransferase subunit 1; 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; IPR054696; GTP-eEF1A_C. 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; PF22594; GTP-eEF1A_C; 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}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000313|EMBL:ABQ61198.1}; 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 24..240 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 33..40 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00062" FT BINDING 112..116 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00062" FT BINDING 167..170 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 644 AA; 71085 MW; 1EA78A7EDF7F7CD8 CRC64; MNVVMKPSQK NTAVADFLAD QEHKSLLRFL TCGSVDDGKS TLIGRLLYDT KLIFEDQLAS LKNDSRKFGT TDDDFDFALL VDGLEAEREQ GITIDVAYRF FSTPRRKFIV ADTPGHAQYT RNMATGASTA DLAVVLVDAR QGVLTQTRRH SFIAAALGIL HIVLAVNKID LVDFSQDRFD GIVADYLSFA QDLGFTSIQP IPLSARFGDN VTASSPRIGW YEGPHLLEHL ETVRIDTEAA AKPFRFPVQY VNRPNLDFRG FSGTVASGSI HVGDPVVVAK SGKQSRVKRI ATYDGDLQRA SEGQAVTLVL EDEIEVSRGN MLAGVELRPE VADRFAADIV WFGEDPLLPG RSYLLRTETD QTPVTVNAIR HRTDVNTFIQ EETARLDLNE IGRCHLQTVD PIAFDPYGEN RATGAFVLID RLTNATVGAG MIDAALRQAT NVHLQAFDLN KQARAAQKFQ KPAVLWFTGL SASGKSTIAN RLEQRLHALG KHTYLLDGDN VRHGLNSDLG FSDADRVENI RRVGEVARLM ADAGLITLVS FISPFREERD QVRARLPEGE FIEIFIDTPI EECMARDPKG LYAQALRGEI KAFTGIDSPY EPPVAPELRL NTAGRTVDEL IAEVENYLAE RGVIGSYGSD SWSI //