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Entry: A0A0Q7ZS98_9ACTN
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ID   A0A0Q7ZS98_9ACTN        Unreviewed;       633 AA.
AC   A0A0Q7ZS98;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 43.
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=cysN {ECO:0000256|HAMAP-Rule:MF_00062};
GN   Synonyms=cysC {ECO:0000256|HAMAP-Rule:MF_00065};
GN   ORFNames=ASD66_00260 {ECO:0000313|EMBL:KQZ74862.1};
OS   Nocardioides sp. Root151.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736475 {ECO:0000313|EMBL:KQZ74862.1, ECO:0000313|Proteomes:UP000051274};
RN   [1] {ECO:0000313|EMBL:KQZ74862.1, ECO:0000313|Proteomes:UP000051274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root151 {ECO:0000313|EMBL:KQZ74862.1,
RC   ECO:0000313|Proteomes:UP000051274};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQZ74862.1, ECO:0000313|Proteomes:UP000051274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root151 {ECO:0000313|EMBL:KQZ74862.1,
RC   ECO:0000313|Proteomes:UP000051274};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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; Evidence={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   -!- 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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00062}.
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:KQZ74862.1}.
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DR   EMBL; LMGG01000001; KQZ74862.1; -; Genomic_DNA.
DR   RefSeq; WP_056889710.1; NZ_LMGG01000001.1.
DR   AlphaFoldDB; A0A0Q7ZS98; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000051274; 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; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
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   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   Pfam; PF03144; GTP_EFTU_D2; 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}; Kinase {ECO:0000256|HAMAP-Rule:MF_00065};
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   Reference proteome {ECO:0000313|Proteomes:UP000051274};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00062}.
FT   DOMAIN          22..238
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   ACT_SITE        541
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         467..474
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
SQ   SEQUENCE   633 AA;  69802 MW;  B2941FAE5D4839C2 CRC64;
     MTHSTDLIAD DIEQYLERHA NKTMLRFITC GSVDDGKSTL IGRLLYESKL VFEDQLTALE
     TDSRKVGTQG EGLDFALLVD GLAAEREQGI TIDVAYRYFS TEQRKFVVAD TPGHEQYTRN
     MVTGASTADL AVILVDARKG VLTQTRRHSF LVSLLGIRHV VLAVNKLDLV DYSQEVFDQI
     VADYSGFAKE IGLDDVVAIP MSAYVGDNLT ERSANTPWYD GPTLIGHLET VQIDDELLTN
     PFRMPVQWVN RPDLDFRGFS GQIVSGVVRP GDRVRVLPSG RESSVSRIVT MDGDLAEAIA
     GQSVTITLAD EIDISRGDVL AIADDLPDVA DQFEAHVVWM GEEEMLPERP YLCQIGTMTV
     QARITKPKHK VNVNTLEKTA TNTLALNEIG VCNLSFDRPV PFDPYAANRD TGGFILIDRL
     TNSTVGAGMI AHSLRRSDNI HWQVVDVDER AREALNGHRP QVLWLTGLSG SGKSTIANHL
     ERRLHALGAH TYLLDGDNIR HGLNRDLGFT EADRVENIRR VTEVARLMAD AGLVVIASFI
     SPFRAEREAA RELVGADQFC EVFVDTPIDV AEGRDPKGLY KKARRGELAN FTGIDSPYEP
     PLAPELRIDT TSVSPEQASD QIVGLLRARG VIS
//
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