CYSN_BACTN
ID CYSN_BACTN Reviewed; 485 AA.
AC Q8AAP9;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=BT_0415;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
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; AE015928; AAO75522.1; -; Genomic_DNA.
DR RefSeq; NP_809328.1; NC_004663.1.
DR RefSeq; WP_011107258.1; NC_004663.1.
DR AlphaFoldDB; Q8AAP9; -.
DR SMR; Q8AAP9; -.
DR STRING; 226186.BT_0415; -.
DR PaxDb; Q8AAP9; -.
DR PRIDE; Q8AAP9; -.
DR EnsemblBacteria; AAO75522; AAO75522; BT_0415.
DR GeneID; 60926373; -.
DR KEGG; bth:BT_0415; -.
DR PATRIC; fig|226186.12.peg.413; -.
DR eggNOG; COG2895; Bacteria.
DR HOGENOM; CLU_007265_5_2_10; -.
DR InParanoid; Q8AAP9; -.
DR OMA; FPVQYVL; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000001414; 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 GO; GO:0006790; P:sulfur compound metabolic process; IBA:GO_Central.
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 Reference proteome; Transferase.
FT CHAIN 1..485
FT /note="Sulfate adenylyltransferase subunit 1"
FT /id="PRO_0000091519"
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 485 AA; 54650 MW; C5514DDBAD87AE88 CRC64;
MDNKLDIKAF LDKDEQKDLL RLLTAGSVDD GKSTLIGRLL FDSKKLYEDQ LDALERDSKR
VGNAGEHIDY ALLLDGLKAE REQGITIDVA YRYFSTNGRK FIIADTPGHE QYTRNMITGG
STANLAIILV DARTGVITQT RRHTFLVSLL GIKHVVLAVN KMDLVDFSEE RFDEIVSEYK
KFVEPLGIPD VNCIPLSALD GDNVVDKSER TPWYKGISLL DFLETVHIDN DHNFTDFRFP
VQYVLRPNLD FRGFCGKVAS GIVRKGDTVM ALPSGKTSKV KSIVTYDGEL DYAFPPQSVT
LTLEDEIDVS RGEMLVHPDN LPIVDRNFEA MMVWMDEEPM DINKSFFIKQ TTNLSRTRID
AIKYKVDVNT MEHLSIDNGQ LTKDNLPLQL NQIARVVLTT AKELFFDPYK KNKSCGSFIL
IDPITNNTSA VGMIIDRVEM KDMAATDDIP VLDLSKLDIA PEHHAAIEKV VKELERQGLS
IKVIK
