(data stored in SCRATCH zone)

SWISSPROT: Q3ILR1_PSEHT

ID   Q3ILR1_PSEHT            Unreviewed;       474 AA.
AC   Q3ILR1;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 99.
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};
GN   Name=cysN {ECO:0000256|HAMAP-Rule:MF_00062,
GN   ECO:0000313|EMBL:CAI85314.1};
GN   OrderedLocusNames=PSHAa0211 {ECO:0000313|EMBL:CAI85314.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85314.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85314.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: May be the GTPase, regulating ATP sulfurylase activity.
CC       {ECO:0000256|HAMAP-Rule:MF_00062, ECO:0000256|SAAS:SAAS00366895}.
CC   -!- CATALYTIC ACTIVITY: ATP + sulfate = diphosphate + adenylyl
CC       sulfate. {ECO:0000256|HAMAP-Rule:MF_00062,
CC       ECO:0000256|SAAS:SAAS00366877}.
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite
CC       from sulfate: step 1/3. {ECO:0000256|HAMAP-Rule:MF_00062,
CC       ECO:0000256|SAAS:SAAS00056006}.
CC   -!- SUBUNIT: Heterodimer composed of CysD, the smaller subunit, and
CC       CysN. {ECO:0000256|HAMAP-Rule:MF_00062,
CC       ECO:0000256|SAAS:SAAS00366889}.
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       ECO:0000256|SAAS:SAAS00558207}.
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DR   EMBL; CR954246; CAI85314.1; -; Genomic_DNA.
DR   RefSeq; WP_011326929.1; NC_007481.1.
DR   ProteinModelPortal; Q3ILR1; -.
DR   STRING; 326442.PSHAa0211; -.
DR   EnsemblBacteria; CAI85314; CAI85314; PSHAa0211.
DR   KEGG; pha:PSHAa0211; -.
DR   PATRIC; fig|326442.8.peg.202; -.
DR   eggNOG; ENOG4105C3T; Bacteria.
DR   eggNOG; COG2895; LUCA.
DR   HOGENOM; HOG000229289; -.
DR   KO; K00956; -.
DR   OMA; SRGDMIC; -.
DR   OrthoDB; POG091H06C6; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_00062; Sulf_adenylyltr_sub1; 1.
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.
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;
DR   PRODOM; Q3ILR1.
DR   SWISS-2DPAGE; Q3ILR1.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS00444459};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS00055993};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS00055970};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS00056011, ECO:0000313|EMBL:CAI85314.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00062,
KW   ECO:0000256|SAAS:SAAS00056018, ECO:0000313|EMBL:CAI85314.1}.
FT   DOMAIN       27    241       Tr-type G (guanine nucleotide-binding).
FT                                {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}.
SQ   SEQUENCE   474 AA;  52409 MW;  B1A891BDB28334DE CRC64;
     MANQNNDTFN EVKAIGIDAY LARQQDKSLL RMLTCGSVDD GKSTLIGRLL HDSHQIYEDQ
     LAALHKDNEK VGNAGDDLDL ALLVDGLQAE REQGITIDVA YRYFSTAKRK FIIADTPGHE
     QYTRNMVTGA STSDVAIILV DARYGVQVQT KRHSFICDSL GIKQFVVAIN KMDIVDFDET
     VYEKIKADYL KFAEQLNVSN IKFVPMSALK GDNVVTRSVH TPYYTDKPLL ELLEDSPAAQ
     IDTDFEARLP VQYVARPNLN FRGFQGTLAS GKLQVGDAIK VLPSGKTSSI KEIVTFDGNL
     DSAQAGQAIT VTLNSEIDIS RGDVIVPASS TAIVTNQLQA KLVWMHETPL QLGKSYNFKL
     GSKNTSAQVT KIDHTIDVNT LEHGSSDTLQ LNEIAIVTLE LSETILADEY HSNHETGSFI
     LIDRLSNLTI AAGMIEQVLQ SQAQQSNFSA FEVEFNTLVR KHFPHWQALD ISKL
//

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