CYSN_PHOLL
ID CYSN_PHOLL Reviewed; 480 AA.
AC Q7N8L0;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=plu0710;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE13005.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX571861; CAE13005.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041379914.1; NC_005126.1.
DR AlphaFoldDB; Q7N8L0; -.
DR SMR; Q7N8L0; -.
DR STRING; 243265.plu0710; -.
DR EnsemblBacteria; CAE13005; CAE13005; plu0710.
DR GeneID; 24167935; -.
DR KEGG; plu:plu0710; -.
DR eggNOG; COG2895; Bacteria.
DR HOGENOM; CLU_007265_5_2_6; -.
DR OrthoDB; 244339at2; -.
DR BioCyc; PLUM243265:PLU_RS03545-MON; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000002514; 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; IPR005225; Small_GTP-bd_dom.
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 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; GTP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..480
FT /note="Sulfate adenylyltransferase subunit 1"
FT /id="PRO_0000091525"
FT DOMAIN 30..248
FT /note="tr-type G"
FT REGION 39..46
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 97..101
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 118..121
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 173..176
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 211..213
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 39..46
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00062"
FT BINDING 118..122
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00062"
FT BINDING 173..176
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00062"
SQ SEQUENCE 480 AA; 53810 MW; 1ED23E674F7EE462 CRC64;
MSALAQNETI AHQIKQQGGV EAYLHAQQEK GLLRFLTCGS VDDGKSTLIG RLLHDTRQIY
EDQLSTLQND SKRIGTQGEK LDLALLVDGL AAEREQGITI DVAYRYFSTE KRKFIIADTP
GHEQYTRNMA TGASTCDLSI LLIDARKGVQ EQTRRHSFIS TLLGIRHLVV AVNKMDLMEY
RQEVFNQIKQ DYMNFAGQLP TNLDVHFVPI SALDGDNIVT ISRNMDWYEG PTLLDILETV
DVKKEASKQL LRFPVQYVSR PDLDFRGYSG TLSSGILRKG QKVKVMPSGI CSQVERIVTF
DGDLDFAVPG EAITVVLKDE IDISRGDLLI SADDEMMVTR HALVDVVWMS EQPLVQGQNL
DIKVAGKKSR GKVENIQYQV DITHLTQRVA VDLPLNAIGS VEFSFEEPLM LDSYQQNSDT
GGIILVDRLT NVTVGAGLVR EIQTDVYEGP KEFSEFELEL NRLIRRHFPH WGARDLLGGK
