位置:首页 > 蛋白库 > HETI_NOSS1
HETI_NOSS1
ID   HETI_NOSS1              Reviewed;         237 AA.
AC   P37695;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=4'-phosphopantetheinyl transferase HetI;
DE            EC=2.7.8.-;
GN   Name=hetI; OrderedLocusNames=all5359;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8157596; DOI=10.1128/jb.176.8.2282-2292.1994;
RA   Black T.A., Wolk C.P.;
RT   "Analysis of a Het- mutation in Anabaena sp. strain PCC 7120 implicates a
RT   secondary metabolite in the regulation of heterocyst spacing.";
RL   J. Bacteriol. 176:2282-2292(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
RN   [3]
RP   PROBABLE FUNCTION.
RX   PubMed=8939709; DOI=10.1016/s1074-5521(96)90181-7;
RA   Lambalot R.H., Gehring A.M., Flugel R.S., Zuber P., LaCelle M.,
RA   Marahiel M.A., Reid R., Khosla C., Walsh C.T.;
RT   "A new enzyme superfamily -- the phosphopantetheinyl transferases.";
RL   Chem. Biol. 3:923-936(1996).
CC   -!- FUNCTION: Probably activates the acyl carrier protein (ACP) domain of
CC       HetM, by transferring the 4'-phosphopantetheinyl moiety of coenzyme A
CC       (CoA) to a serine residue. May be required for maintaining vegetative
CC       growth and probably acts via HetN to inhibit differentiation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=apo-[peptidyl-carrier protein] + CoA = adenosine 3',5'-
CC         bisphosphate + H(+) + holo-[peptidyl-carrier protein];
CC         Xref=Rhea:RHEA:46228, Rhea:RHEA-COMP:11479, Rhea:RHEA-COMP:11480,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:64479;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the P-Pant transferase superfamily.
CC       Gsp/Sfp/HetI/AcpT family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB77058.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L22883; AAA22003.1; -; Genomic_DNA.
DR   EMBL; BA000019; BAB77058.1; ALT_INIT; Genomic_DNA.
DR   PIR; AG2475; AG2475.
DR   PIR; E55210; E55210.
DR   RefSeq; WP_044522635.1; NZ_RSCN01000005.1.
DR   AlphaFoldDB; P37695; -.
DR   SMR; P37695; -.
DR   STRING; 103690.17134498; -.
DR   EnsemblBacteria; BAB77058; BAB77058; BAB77058.
DR   KEGG; ana:all5359; -.
DR   eggNOG; COG2091; Bacteria.
DR   OMA; RYWTCKE; -.
DR   OrthoDB; 1542506at2; -.
DR   Proteomes; UP000002483; Chromosome.
DR   GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   Gene3D; 3.90.470.20; -; 2.
DR   InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR   InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR   Pfam; PF01648; ACPS; 1.
DR   SUPFAM; SSF56214; SSF56214; 2.
PE   3: Inferred from homology;
KW   Magnesium; Metal-binding; Reference proteome; Transferase.
FT   CHAIN           1..237
FT                   /note="4'-phosphopantetheinyl transferase HetI"
FT                   /id="PRO_0000206075"
FT   BINDING         128
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   237 AA;  27108 MW;  06EABCDC73E23873 CRC64;
     MLQHTWLPKP PNLTLLSDEV HLWRIPLDQP ESQLQDLAAT LSSDELARAN RFYFPEHRRR
     FTAGRGILRS ILGGYLGVEP GQVKFDYESR GKPILGDRFA ESGLLFNLSH SQNLALCAVN
     YTRQIGIDLE YLRPTSDLES LAKRFFLPRE YELLRSLPDE QKQKIFFRYW TCKEAYLKAT
     GDGIAKLEEI EIALTPTEPA KLQTAPAWSL LELVPDDNCV AAVAVAGFGW QPKFWHY
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024