ID A0A2A2EQ13_9GAMM Unreviewed; 644 AA. AC A0A2A2EQ13; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 05-DEC-2018, entry version 8. 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 sp. WRN001. OC Bacteria; Proteobacteria; 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: 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:SAAS00366877}; 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:456216, ChEBI:CHEBI:58243, CC ChEBI:CHEBI:58339; 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: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 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: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 Complete proteome {ECO:0000313|Proteomes:UP000217771}; 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:PAU74748.1}; 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:PAU74748.1}; KW Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00062, KW ECO:0000256|SAAS:SAAS00056018, ECO:0000313|EMBL:PAU74748.1}. FT DOMAIN 22 245 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 484 491 ATP. {ECO:0000256|HAMAP-Rule:MF_00065}. FT ACT_SITE 558 558 Phosphoserine intermediate. FT {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 //