ID A0A2A2EQ13_9GAMM Unreviewed; 644 AA. AC A0A2A2EQ13; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 24-JAN-2024, entry version 24. 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=cysC {ECO:0000256|HAMAP-Rule:MF_00065}; GN Synonyms=cysN {ECO:0000256|HAMAP-Rule:MF_00062}; GN ORFNames=CK498_21750 {ECO:0000313|EMBL:PAU74748.1}; OS Halomonas salipaludis. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=2032625 {ECO:0000313|EMBL:PAU74748.1, ECO:0000313|Proteomes:UP000217771}; RN [1] {ECO:0000313|EMBL:PAU74748.1, ECO:0000313|Proteomes:UP000217771} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WRN001 {ECO:0000313|EMBL:PAU74748.1, RC ECO:0000313|Proteomes:UP000217771}; RA Wang D., Zhang G.; RT "Halomonas alkalisoli sp. nov., isolated from saline alkaline soil."; RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases. 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: 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|ARBA:ARBA00004806, ECO:0000256|HAMAP- CC 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 -!- 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PAU74748.1}. 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; NSKB01000009; PAU74748.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2A2EQ13; -. DR OrthoDB; 9804504at2; -. DR UniPathway; UPA00140; UER00204. DR Proteomes; UP000217771; Unassembled WGS sequence. 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 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; 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 NCBIfam; TIGR00455; apsK; 1. DR NCBIfam; TIGR02034; CysN; 1. DR NCBIfam; TIGR00231; small_GTP; 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}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000313|EMBL:PAU74748.1}; 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 22..245 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" FT ACT_SITE 558 FT /note="Phosphoserine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065" FT BINDING 31..38 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00062" FT BINDING 110..114 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00062" FT BINDING 165..168 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00062" FT BINDING 484..491 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065" SQ SEQUENCE 644 AA; 71152 MW; EF314788A5EF24BE CRC64; MSHSSPLIAD DIESYLKEHE NKDLLRFITC GSVDDGKSTL IGRLLHDSKM IYEDQLAAIT QASKTSGTTG DAVDLALLVD GLQSEREQGI TIDVAYRFFS TDKRKFIIAD TPGHEQYTRN MATGASTASL AIILIDARYG VQTQTRRHSF IADLLGIQHL VIAINKMDLV EFSEARYDEI VAQYQEVAAK LHAPDIRFIP LSALNGDNVV DPSQHTPWYR DASGAPGATL LQLLESVEIT HDQNLSDLRF PVQYVNRPNL DFRGYCGTLA AGILRPGQAV KALPSGKTSS VERIVTYDGD LDVAYPGQAI TLTLADEIDI SRGDWLVSAD AEVPLVVGFE ADIVWMHDTA LEPGKLYDLK LATRDLAGKV TAIDYQIDVN TLEHRHAEHL DLNSIARCSV ELTAPVPVDD YRKSPGTGSF IIIDRLTNVT VGAGMIHQPS DSETPYEYRA HDSKANVVWN RTSVTQAMRE QLNGHSGKCI WFTGLSGSGK STLANALEIE LNRRGYHTML LDGDNVRHGL CKDLGMGEED RGENIRRVGE VARLFAEAGI IVITAFISPF RKDRDAVRAL FDEDAFIEVH VDTPLDVCEQ RDPKGLYQKA REGKIKDFTG IDSPYEPPVH GEIVLKTMFD NEQALISKVI KHVL //