CYSN_BACFR
ID CYSN_BACFR Reviewed; 476 AA.
AC Q64VQ9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Sulfate adenylyltransferase subunit 1 {ECO:0000255|HAMAP-Rule:MF_00062};
DE EC=2.7.7.4 {ECO:0000255|HAMAP-Rule:MF_00062};
DE AltName: Full=ATP-sulfurylase large subunit {ECO:0000255|HAMAP-Rule:MF_00062};
DE AltName: Full=Sulfate adenylate transferase {ECO:0000255|HAMAP-Rule:MF_00062};
DE Short=SAT {ECO:0000255|HAMAP-Rule:MF_00062};
GN Name=cysN {ECO:0000255|HAMAP-Rule:MF_00062}; OrderedLocusNames=BF1669;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_00062};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3. {ECO:0000255|HAMAP-Rule:MF_00062}.
CC -!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and CysN.
CC {ECO:0000255|HAMAP-Rule:MF_00062}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. CysN/NodQ
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00062}.
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DR EMBL; AP006841; BAD48417.1; -; Genomic_DNA.
DR RefSeq; WP_005786535.1; NC_006347.1.
DR RefSeq; YP_098951.1; NC_006347.1.
DR AlphaFoldDB; Q64VQ9; -.
DR SMR; Q64VQ9; -.
DR STRING; 295405.BF1669; -.
DR EnsemblBacteria; BAD48417; BAD48417; BF1669.
DR GeneID; 66329501; -.
DR KEGG; bfr:BF1669; -.
DR PATRIC; fig|295405.11.peg.1621; -.
DR HOGENOM; CLU_007265_5_2_10; -.
DR OMA; FPVQYVL; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000002197; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd04166; CysN_ATPS; 1.
DR CDD; cd03695; CysN_NodQ_II; 1.
DR CDD; cd04095; CysN_NoDQ_III; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00062; Sulf_adenylyltr_sub1; 1.
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 Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02034; CysN; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; GTP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Transferase.
FT CHAIN 1..476
FT /note="Sulfate adenylyltransferase subunit 1"
FT /id="PRO_1000092134"
FT DOMAIN 17..232
FT /note="tr-type G"
FT REGION 26..33
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 84..88
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 105..108
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 160..163
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 197..199
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 26..33
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00062"
FT BINDING 105..109
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00062"
FT BINDING 160..163
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00062"
SQ SEQUENCE 476 AA; 53705 MW; BB7837D590B28CA5 CRC64;
MADKLDIKAF LDKDEQKDLL RLLTAGSVDD GKSTLIGRLL FDSKKLYEDQ LDALERDSKR
LGNAGEHIDY ALLLDGLKAE REQGITIDVA YRYFSTNNRK FIIADTPGHE QYTRNMITGG
STANLAIILV DARMGVITQT RRHTFLVSLL GIKHVVLAVN KMDLVDFSEE RFNEIVAEYK
KFVAPLGIPD VTCIPLSALD GDNVVDKSER TPWYEGLSLL DFLETVHIDS DNNFSDFRFP
VQYVLRPNLD FRGFCGKVAS GIIRKGDKVM ALPSGKVSHV KSIVTFDGEL DYAFPPQSVT
LTLEDEIDVS RGEMLVHPDN LPIVDRNFEA MLVWMDEEPM DINKSFFIKQ TTNVSRTRID
SIKYKVDVNT MEHSSVPFLS LNEIARVVFT TAKELFFDPY RKNKSCGSFI LIDPITNNTS
AVGMIIDRVE KKDMNIADDF PVLNLPELGI APEHYEAIEK AVKSLSEQGF EVRIEK
