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PSEH_HELPY
ID   PSEH_HELPY              Reviewed;         180 AA.
AC   O25094;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase;
DE            EC=2.3.1.202;
DE   AltName: Full=Pseudaminic acid biosynthesis protein H;
GN   Name=pseH; OrderedLocusNames=HP_0327;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=16751642; DOI=10.1093/glycob/cwl010;
RA   Schoenhofen I.C., McNally D.J., Brisson J.R., Logan S.M.;
RT   "Elucidation of the CMP-pseudaminic acid pathway in Helicobacter pylori:
RT   synthesis from UDP-N-acetylglucosamine by a single enzymatic reaction.";
RL   Glycobiology 16:8C-14C(2006).
CC   -!- FUNCTION: Catalyzes the third step in the biosynthesis of pseudaminic
CC       acid, a sialic-acid-like sugar that is used to modify flagellin.
CC       Mediates N-4 acetylation of UDP-4-amino-4,6-dideoxy-beta-L-AltNAc to
CC       form UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose.
CC       {ECO:0000269|PubMed:16751642}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-
CC         altrosamine = CoA + H(+) + UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-
CC         altrose; Xref=Rhea:RHEA:34155, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:63389, ChEBI:CHEBI:63417;
CC         EC=2.3.1.202; Evidence={ECO:0000269|PubMed:16751642};
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DR   EMBL; AE000511; AAD07394.1; -; Genomic_DNA.
DR   PIR; G64560; G64560.
DR   RefSeq; NP_207125.1; NC_000915.1.
DR   RefSeq; WP_000742697.1; NC_018939.1.
DR   PDB; 4RI1; X-ray; 2.30 A; A/B/C=1-180.
DR   PDBsum; 4RI1; -.
DR   AlphaFoldDB; O25094; -.
DR   SMR; O25094; -.
DR   DIP; DIP-3555N; -.
DR   IntAct; O25094; 4.
DR   MINT; O25094; -.
DR   STRING; 85962.C694_01655; -.
DR   PaxDb; O25094; -.
DR   DNASU; 900098; -.
DR   EnsemblBacteria; AAD07394; AAD07394; HP_0327.
DR   KEGG; hpy:HP_0327; -.
DR   PATRIC; fig|85962.8.peg.341; -.
DR   eggNOG; COG1670; Bacteria.
DR   OMA; NHYELEG; -.
DR   PhylomeDB; O25094; -.
DR   BioCyc; MetaCyc:HP0327-MON; -.
DR   BRENDA; 2.3.1.202; 2604.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR020036; PseH.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   TIGRFAMs; TIGR03585; PseH; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..180
FT                   /note="UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine
FT                   N-acetyltransferase"
FT                   /id="PRO_0000418961"
FT   DOMAIN          13..169
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   STRAND          5..7
FT                   /evidence="ECO:0007829|PDB:4RI1"
FT   STRAND          10..14
FT                   /evidence="ECO:0007829|PDB:4RI1"
FT   HELIX           15..17
FT                   /evidence="ECO:0007829|PDB:4RI1"
FT   HELIX           20..31
FT                   /evidence="ECO:0007829|PDB:4RI1"
FT   HELIX           33..36
FT                   /evidence="ECO:0007829|PDB:4RI1"
FT   STRAND          39..42
FT                   /evidence="ECO:0007829|PDB:4RI1"
FT   HELIX           46..56
FT                   /evidence="ECO:0007829|PDB:4RI1"
FT   STRAND          63..69
FT                   /evidence="ECO:0007829|PDB:4RI1"
FT   STRAND          72..83
FT                   /evidence="ECO:0007829|PDB:4RI1"
FT   TURN            84..87
FT                   /evidence="ECO:0007829|PDB:4RI1"
FT   STRAND          88..95
FT                   /evidence="ECO:0007829|PDB:4RI1"
FT   HELIX           103..115
FT                   /evidence="ECO:0007829|PDB:4RI1"
FT   STRAND          121..128
FT                   /evidence="ECO:0007829|PDB:4RI1"
FT   HELIX           132..140
FT                   /evidence="ECO:0007829|PDB:4RI1"
FT   STRAND          144..155
FT                   /evidence="ECO:0007829|PDB:4RI1"
FT   STRAND          158..168
FT                   /evidence="ECO:0007829|PDB:4RI1"
FT   HELIX           169..177
FT                   /evidence="ECO:0007829|PDB:4RI1"
SQ   SEQUENCE   180 AA;  21353 MW;  2565A24C8C770DCA CRC64;
     MKKNYSYKNI QAIDFTNLND GEKLLVLEFR NHPNTALWMY STFISLKTHL QFIEDLKNSP
     NHRYFLFKEE GVYLGVGSIT KINFFHKHGY LGIYKNPFLK NGGETILKAL EFIAFEEFQL
     HSLHLEVMEN NFKAIAFYEK NHYELEGRLK GFISKDKEFI DVLLYYKDKK GYNDQSLLKL
 
 
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