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CYSNC_XYLFA
ID   CYSNC_XYLFA             Reviewed;         623 AA.
AC   Q9PD78;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Bifunctional enzyme CysN/CysC;
DE   Includes:
DE     RecName: Full=Sulfate adenylyltransferase subunit 1;
DE              EC=2.7.7.4;
DE     AltName: Full=ATP-sulfurylase large subunit;
DE     AltName: Full=Sulfate adenylate transferase;
DE              Short=SAT;
DE   Includes:
DE     RecName: Full=Adenylyl-sulfate kinase;
DE              EC=2.7.1.25;
DE     AltName: Full=APS kinase;
DE     AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase;
GN   Name=cysNC; OrderedLocusNames=XF_1501;
OS   Xylella fastidiosa (strain 9a5c).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=160492;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9a5c;
RX   PubMed=10910347; DOI=10.1038/35018003;
RA   Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M.,
RA   Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S.,
RA   Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S.,
RA   Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H.,
RA   Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M.,
RA   Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H.,
RA   Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S.,
RA   Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H.,
RA   Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D.,
RA   Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E.,
RA   Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F.,
RA   Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N.,
RA   Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F.,
RA   Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y.,
RA   Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O.,
RA   Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A.,
RA   de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R.,
RA   Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B.,
RA   Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G.,
RA   Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M.,
RA   da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z.,
RA   Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D.,
RA   Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S.,
RA   Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.;
RT   "The genome sequence of the plant pathogen Xylella fastidiosa.";
RL   Nature 406:151-159(2000).
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:0000250}.
CC   -!- FUNCTION: APS kinase catalyzes the synthesis of activated sulfate.
CC       {ECO:0000250}.
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;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate
CC         + 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;
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 1/3.
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 2/3.
CC   -!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and CysNC.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the APS kinase
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the TRAFAC class
CC       translation factor GTPase superfamily. Classic translation factor
CC       GTPase family. CysN/NodQ subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF84310.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE003849; AAF84310.1; ALT_INIT; Genomic_DNA.
DR   PIR; G82672; G82672.
DR   AlphaFoldDB; Q9PD78; -.
DR   SMR; Q9PD78; -.
DR   STRING; 160492.XF_1501; -.
DR   EnsemblBacteria; AAF84310; AAF84310; XF_1501.
DR   KEGG; xfa:XF_1501; -.
DR   eggNOG; COG0529; Bacteria.
DR   eggNOG; COG2895; Bacteria.
DR   HOGENOM; CLU_007265_5_1_6; -.
DR   OMA; PGHVEYT; -.
DR   UniPathway; UPA00140; UER00204.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000000812; Chromosome.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR   CDD; cd02027; APSK; 1.
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; -; 2.
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; 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; 2.
DR   TIGRFAMs; TIGR00455; apsK; 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; Kinase; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..623
FT                   /note="Bifunctional enzyme CysN/CysC"
FT                   /id="PRO_0000091539"
FT   DOMAIN          14..228
FT                   /note="tr-type G"
FT   REGION          1..450
FT                   /note="Sulfate adenylyltransferase"
FT   REGION          23..30
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          81..85
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          102..105
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          157..160
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          194..196
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   REGION          451..623
FT                   /note="Adenylyl-sulfate kinase"
FT   ACT_SITE        533
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         23..30
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         102..106
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         157..160
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         459..466
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   623 AA;  68278 MW;  C20730A365B28E94 CRC64;
     MQSVIADLKQ QEIKPLLRFI TCGSVDDGKS TLIGHLLYDS QCLAEDQLAD LMVDSQRYGT
     QGEHIDYALL LDGLAAEREQ GITIDVAYRY FDTEKRKFIV ADCPGHAQYT RNMATGASTA
     DAAVVLVDAR KGLLTQTRRH SYIVALLGIR HVVLAVNKMD LVGYDQETFE AIASDYLALA
     AKLGINQVQC IPLSALEGDN LSKRSARMPW YVGPSLLEYL EALEPADVDL AAAMCLPVQW
     VNRPDSQFRG FTGTLAAGRV RPGDAVVVLP SGCVSRVVRV FNGDTEVHEA VAGQAVTLTL
     ADEIDISRGD VIAALDDPPE VADQVTAYVL WMDDTALLPG RRYWLKLGAR MVAASVSDIK
     HRVDVNTQEQ RVAQRLQLNE VGYCQLSLDA PVAFVPYARN RVLGSFILID RHSNATVGAG
     TLDSGVHRAS NVHWQPLDID HVARARIKGQ TPKVLWFTGL SGAGKSAIAN IVDKRLHALG
     YHTFILDGDN VRHGLNRDLS FTVEDRVENI RRVAEVARLM VDAGLVVLVS FISPFRDERQ
     LARERFAANE FVEVFVDVPL AVAEARDVKG LYAKARAGLI TDFTGIDSPY EPPPHPELHL
     RADQGTPEQL ASQVLSFLGV EAN
 
 
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