ID   A0A436SZZ6_9RHIZ        Unreviewed;       647 AA.
AC   A0A436SZZ6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   03-JUL-2019, entry version 3.
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   ECO:0000313|EMBL:RVC87265.1};
GN   Synonyms=cysC {ECO:0000256|HAMAP-Rule:MF_00065};
GN   ORFNames=EN874_15180 {ECO:0000313|EMBL:RVC87265.1};
OS   Mesorhizobium sp. M1D.F.Ca.ET.231.01.1.1.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=2496669 {ECO:0000313|EMBL:RVC87265.1, ECO:0000313|Proteomes:UP000282996};
RN   [1] {ECO:0000313|EMBL:RVC87265.1, ECO:0000313|Proteomes:UP000282996}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1D.F.Ca.ET.231.01.1.1 {ECO:0000313|EMBL:RVC87265.1,
RC   ECO:0000313|Proteomes:UP000282996};
RA   Greenlon A., Chang P.L., Cook D.R.;
RT   "Global Population Genomics of Chickpea-Nodulating Mesorhizobium.";
RL   Submitted (NOV-2018) 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:SAAS01159104};
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: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
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:RVC87265.1}.
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DR   EMBL; RZOZ01000006; RVC87265.1; -; Genomic_DNA.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000282996; 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   CDD; cd04166; CysN_ATPS; 1.
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; 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:SAAS01159110};
KW   Complete proteome {ECO:0000313|Proteomes:UP000282996};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS01159120};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00065,
KW   ECO:0000256|SAAS:SAAS01092249};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS01159098};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS01159099, ECO:0000313|EMBL:RVC87265.1};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS01159119, ECO:0000313|EMBL:RVC87265.1}.
FT   DOMAIN       27    242       Tr-type G. {ECO:0000259|PROSITE:PS51722}.
FT   NP_BIND      36     43       GTP. {ECO:0000256|HAMAP-Rule:MF_00062}.
FT   NP_BIND     115    119       GTP. {ECO:0000256|HAMAP-Rule:MF_00062}.
FT   NP_BIND     170    173       GTP. {ECO:0000256|HAMAP-Rule:MF_00062}.
FT   NP_BIND     472    479       ATP. {ECO:0000256|HAMAP-Rule:MF_00065}.
FT   ACT_SITE    546    546       Phosphoserine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00065}.
SQ   SEQUENCE   647 AA;  71335 MW;  2C2876C0DF2465C0 CRC64;
     MTMRHIMAKS LAPTDSIRDY MASQEKKSLL RFLTCGSVDD GKSTLIGRLL SDTKQIFEDQ
     LAALENDSRK HGTTGDDIDF ALLVDGLEAE REQGITIDVA YRFFATPKRK FIVADTPGHE
     QYTRNMATGA STADLAIVLI DARQGVLRQT RRHSIIASLL GIRHIVLAVN KIDLVGFDKT
     VFDKIVADYG DFAKGLGFAS IVPIPMSARF GDNVTSRSER SPWYSGPSLI EHLEIVSVDE
     AAVELPFRFP VQYVNRPNLD FRGFAGTIAS GTVSQGDEVV VAKSGRASRV RRIVAHGGDL
     EQAVAGQAIT LVLEDEVEVS RGNMLVSPAA RPQVADQFAA NIVWFDEQAL LPGRSYILRT
     ETDQVSATVT ELKYRVNVND FAHEAAKSLD LNEVGVCNLS TRAPIAFDPF AENRTTGAFI
     LIDRISNATV GAGMILHSLR RAENIHWQSL DVGKRGRSDL KNQRPAVFWF TGLSGSGKST
     IANLFERKLF ASGRHTYILD GDNVRHGLNR DLGFTDADRV ENIRRVAEVA KLMADAGLIV
     IVSFISPFSA ERRMARELMG EGEFVEVFVD TPFEECARRD PKGLYARALS GEIKNFTGVD
     SPYEAPENPE IHLETLGRSP QEMAEALEHW LTERDIAEEQ YDNGGGI
//