ID   A0A2A2EQ13_9GAMM        Unreviewed;       644 AA.
AC   A0A2A2EQ13;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   22-FEB-2023, entry version 21.
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; 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: 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}.
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DR   EMBL; NSKB01000009; PAU74748.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2EQ13; -.
DR   EnsemblBacteria; PAU74748; PAU74748; CK498_21750.
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   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   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|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
//