ID Q8GBT1_RHISB Unreviewed; 627 AA.
AC Q8GBT1;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 13-SEP-2023, entry version 99.
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=nodQ2 {ECO:0000313|EMBL:CAD57728.1};
GN Synonyms=cysC {ECO:0000256|HAMAP-Rule:MF_00065}, cysN
GN {ECO:0000256|HAMAP-Rule:MF_00062};
OS Rhizobium sp. (strain BR816).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Ensifer.
OX NCBI_TaxID=1057002 {ECO:0000313|EMBL:CAD57728.1};
RN [1] {ECO:0000313|EMBL:CAD57728.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BR816 {ECO:0000313|EMBL:CAD57728.1};
RX PubMed=7986038;
RA van Rhijn P., Desair J., Vlassak K., Vanderleyden J.;
RT "The NodD proteins of Rhizobium sp. strain BR816 differ in their
RT interactions with coinducers and in their activities for nodulation of
RT different host plants.";
RL Appl. Environ. Microbiol. 60:3615-3623(1994).
RN [2] {ECO:0000313|EMBL:CAD57728.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BR816 {ECO:0000313|EMBL:CAD57728.1};
RX PubMed=12676676; DOI=10.1128/AEM.69.4.2006-2014.2003;
RA Snoeck C., Verreth C., Hernandez-Lucas I., Martinez-Romero E.,
RA Vanderleyden J.;
RT "Identification of a third sulfate activation system in Sinorhizobium sp.
RT strain BR816: the CysDN sulfate activation complex.";
RL Appl. Environ. Microbiol. 69:2006-2014(2003).
RN [3] {ECO:0000313|EMBL:CAD57728.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BR816 {ECO:0000313|EMBL:CAD57728.1};
RX PubMed=17233732; DOI=10.1111/j.1574-6968.2006.00521.x;
RA Remans R., Snoeck C., Verreth C., Croonenborghs A., Luyten E.,
RA Ndayizeye M., Martinez-Romero E., Michiels J., Vanderleyden J.;
RT "Inactivation of the nodH gene in Sinorhizobium sp. BR816 enhances
RT symbiosis with Phaseolus vulgaris L.";
RL FEMS Microbiol. Lett. 266:210-217(2007).
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=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|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; AJ518946; CAD57728.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8GBT1; -.
DR UniPathway; UPA00140; UER00204.
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; 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 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00062}.
FT DOMAIN 19..231
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT ACT_SITE 535
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
FT BINDING 28..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00062"
FT BINDING 104..108
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00062"
FT BINDING 159..162
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00062"
FT BINDING 461..468
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
SQ SEQUENCE 627 AA; 69219 MW; 6232777B13E2CD21 CRC64;
MLSIPPHDIE ARLAEHDNKS ILRFITCGSV DDGKSTLIGR LLYDAKLIFE DQLANLGRVG
VANGEEIDLS LLLDGLEAER EQGITIDVAY RYFATSKRKF IVADTPGHEE YTRNMVTGAS
TADLAVILID GRQGILQQTR RHSCIASLLG IRHVVLAVNK IDLVDFRQQV FDEIVADYLA
FARELGFASI RPIPISARYG DNVVSASANT SWYKGPALLE YLETVQVDPP TQEKPFRFPV
QLVLRPNADF RGYAGQAASG HVTVGDPVVV AKSGQRTTVK AIVTYDGNLE RAGEGEAVTL
VLADEVDASR GNMLVAPAAR RFVADQFQAH VIWFDASPMF PGRSYILRTE TDSVSATVTT
LKHQVNVNSF AREAAKSLQM NEVGVCNIST QVPIAFDAYK DNRATGNFII VDRVTNATVG
AGLIDFPLRR ADNVHWQAFE VNKAARSAMK SQRATVLWFT GLSGSGKSTI GNALDRILHA
RGKHTYLLDG DNVRHGLNRD LGFTEEDRVE NIRRVAEVAK LMADAGLIVL VSFISPFRDE
RRMARELMDE GEFIEIFVDT PIEECARRDP KGLYEKALAG KIANFTGVSS PYEVPESPEL
HLKTVEVDPV ALALKIEEFL DQRMEEK
//
