ID A0A436SZZ6_9RHIZ Unreviewed; 647 AA.
AC A0A436SZZ6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 05-JUN-2019, entry version 2.
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 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
//