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NANM_ECOLI
ID   NANM_ECOLI              Reviewed;         368 AA.
AC   P39371; Q2M603;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=N-acetylneuraminate epimerase;
DE            EC=5.1.3.24 {ECO:0000269|PubMed:33895133};
DE   AltName: Full=N-acetylneuraminate anomerase NanM {ECO:0000303|PubMed:33895133};
DE   AltName: Full=N-acetylneuraminate mutarotase;
DE            Short=Neu5Ac mutarotase;
DE   AltName: Full=Sialic acid epimerase;
DE   Flags: Precursor;
GN   Name=nanM; Synonyms=yjhT; OrderedLocusNames=b4310, JW5777;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT   from 92.8 through 100 minutes.";
RL   Nucleic Acids Res. 23:2105-2119(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   INDUCTION BY SIALIC ACID.
RX   PubMed=15743943; DOI=10.1128/jb.187.6.1959-1965.2005;
RA   Condemine G., Berrier C., Plumbridge J., Ghazi A.;
RT   "Function and expression of an N-acetylneuraminic acid-inducible outer
RT   membrane channel in Escherichia coli.";
RL   J. Bacteriol. 187:1959-1965(2005).
RN   [5]
RP   INDUCTION.
RX   PubMed=23935044; DOI=10.1128/jb.00692-13;
RA   Kalivoda K.A., Steenbergen S.M., Vimr E.R.;
RT   "Control of the Escherichia coli sialoregulon by transcriptional repressor
RT   NanR.";
RL   J. Bacteriol. 195:4689-4701(2013).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RC   STRAIN=K12;
RX   PubMed=33895133; DOI=10.1016/j.jbc.2021.100699;
RA   Kentache T., Thabault L., Deumer G., Haufroid V., Frederick R.,
RA   Linster C.L., Peracchi A., Veiga-da-Cunha M., Bommer G.T.,
RA   Van Schaftingen E.;
RT   "The metalloprotein YhcH is an anomerase providing N-acetylneuraminate
RT   aldolase with the open form of its substrate.";
RL   J. Biol. Chem. 296:100699-100699(2021).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), NMR, MASS SPECTROMETRY, FUNCTION,
RP   SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF LYS-30; GLU-228; ARG-234;
RP   HIS-297; LYS-302; TYR-328 AND GLU-344.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=18063573; DOI=10.1074/jbc.m707822200;
RA   Severi E., Mueller A., Potts J.R., Leech A., Williamson D., Wilson K.S.,
RA   Thomas G.H.;
RT   "Sialic acid mutarotation is catalyzed by the Escherichia coli beta-
RT   propeller protein YjhT.";
RL   J. Biol. Chem. 283:4841-4849(2008).
CC   -!- FUNCTION: Converts alpha-N-acetylneuranimic acid (Neu5Ac) to the beta-
CC       anomer, accelerating the equilibrium between the alpha- and beta-
CC       anomers. Probably facilitates sialidase-negative bacteria to compete
CC       sucessfully for limited amounts of extracellular Neu5Ac, which is
CC       likely taken up in the beta-anomer. In addition, the rapid removal of
CC       sialic acid from solution might be advantageous to the bacterium to
CC       damp down host responses (PubMed:18063573). Forms linear aceneuramate
CC       during interconversion of Neu5Ac anomers (PubMed:33895133).
CC       {ECO:0000269|PubMed:18063573, ECO:0000269|PubMed:33895133}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-alpha-neuraminate = N-acetyl-beta-neuraminate;
CC         Xref=Rhea:RHEA:25233, ChEBI:CHEBI:58705, ChEBI:CHEBI:58770;
CC         EC=5.1.3.24; Evidence={ECO:0000269|PubMed:33895133};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25234;
CC         Evidence={ECO:0000269|PubMed:33895133};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25235;
CC         Evidence={ECO:0000269|PubMed:33895133};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18063573}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:18063573}.
CC   -!- INDUCTION: Induced by N-acetylneuraminate and modulated by N-
CC       acetylglucosamine, via the NanR and NagC regulators.
CC       {ECO:0000269|PubMed:15743943, ECO:0000269|PubMed:23935044}.
CC   -!- MASS SPECTROMETRY: Mass=38685; Mass_error=4; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:18063573};
CC   -!- SIMILARITY: Belongs to the NanM family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA97206.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U14003; AAA97206.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC77266.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78303.1; -; Genomic_DNA.
DR   PIR; S56535; S56535.
DR   RefSeq; NP_418730.4; NC_000913.3.
DR   RefSeq; WP_001309184.1; NZ_SSUV01000012.1.
DR   PDB; 2UVK; X-ray; 1.50 A; A/B=20-368.
DR   PDBsum; 2UVK; -.
DR   AlphaFoldDB; P39371; -.
DR   SMR; P39371; -.
DR   BioGRID; 4259377; 10.
DR   DIP; DIP-12628N; -.
DR   IntAct; P39371; 6.
DR   STRING; 511145.b4310; -.
DR   jPOST; P39371; -.
DR   PaxDb; P39371; -.
DR   PRIDE; P39371; -.
DR   EnsemblBacteria; AAC77266; AAC77266; b4310.
DR   EnsemblBacteria; BAE78303; BAE78303; BAE78303.
DR   GeneID; 949106; -.
DR   KEGG; ecj:JW5777; -.
DR   KEGG; eco:b4310; -.
DR   PATRIC; fig|1411691.4.peg.2383; -.
DR   EchoBASE; EB2450; -.
DR   eggNOG; COG3055; Bacteria.
DR   HOGENOM; CLU_061535_0_0_6; -.
DR   InParanoid; P39371; -.
DR   OMA; PSTNKWR; -.
DR   PhylomeDB; P39371; -.
DR   BioCyc; EcoCyc:G7920-MON; -.
DR   BioCyc; MetaCyc:G7920-MON; -.
DR   BRENDA; 5.1.3.24; 2026.
DR   EvolutionaryTrace; P39371; -.
DR   PRO; PR:P39371; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR   GO; GO:0016857; F:racemase and epimerase activity, acting on carbohydrates and derivatives; IDA:EcoCyc.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.120.10.80; -; 2.
DR   HAMAP; MF_01195; NanM; 1.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR019936; Mutatrotase_YjhT-like.
DR   SUPFAM; SSF117281; SSF117281; 1.
DR   TIGRFAMs; TIGR03547; muta_rot_YjhT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Isomerase; Kelch repeat; Periplasm;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL          1..19
FT   CHAIN           20..368
FT                   /note="N-acetylneuraminate epimerase"
FT                   /id="PRO_0000016655"
FT   REPEAT          40..84
FT                   /note="Kelch 1"
FT   REPEAT          86..137
FT                   /note="Kelch 2"
FT   REPEAT          139..173
FT                   /note="Kelch 3"
FT   REPEAT          174..219
FT                   /note="Kelch 4"
FT   REPEAT          222..265
FT                   /note="Kelch 5"
FT   REPEAT          287..336
FT                   /note="Kelch 6"
FT   REPEAT          338..367
FT                   /note="Kelch 7"
FT   ACT_SITE        228
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         30
FT                   /note="K->A: No effect on catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:18063573"
FT   MUTAGEN         228
FT                   /note="E->A: Great decrease in catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:18063573"
FT   MUTAGEN         234
FT                   /note="R->A: Decrease in catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:18063573"
FT   MUTAGEN         297
FT                   /note="H->A: No effect on catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:18063573"
FT   MUTAGEN         302
FT                   /note="K->A: No effect on catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:18063573"
FT   MUTAGEN         328
FT                   /note="Y->A: No effect on catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:18063573"
FT   MUTAGEN         344
FT                   /note="E->A: No effect on catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:18063573"
FT   STRAND          33..37
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          40..44
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   HELIX           46..48
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          52..56
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          64..66
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          79..83
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          86..90
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          93..95
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          101..103
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          107..111
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   TURN            112..115
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          116..119
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          132..136
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          139..143
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   HELIX           148..161
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   HELIX           165..176
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   HELIX           180..183
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          188..192
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   TURN            194..196
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          199..204
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          214..218
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          221..225
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          228..230
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          238..242
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          245..247
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          249..252
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   TURN            258..260
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          266..270
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          273..277
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   HELIX           285..290
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   TURN            296..299
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          307..310
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          317..321
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          327..334
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          337..344
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   HELIX           346..348
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          350..358
FT                   /evidence="ECO:0007829|PDB:2UVK"
FT   STRAND          365..367
FT                   /evidence="ECO:0007829|PDB:2UVK"
SQ   SEQUENCE   368 AA;  39572 MW;  1194F392C51EA204 CRC64;
     MNKTITALAI MMASFAANAS VLPETPVPFK SGTGAIDNDT VYIGLGSAGT AWYKLDTQAK
     DKKWTALAAF PGGPRDQATS AFIDGNLYVF GGIGKNSEGL TQVFNDVHKY NPKTNSWVKL
     MSHAPMGMAG HVTFVHNGKA YVTGGVNQNI FNGYFEDLNE AGKDSTAIDK INAHYFDKKA
     EDYFFNKFLL SFDPSTQQWS YAGESPWYGT AGAAVVNKGD KTWLINGEAK PGLRTDAVFE
     LDFTGNNLKW NKLAPVSSPD GVAGGFAGIS NDSLIFAGGA GFKGSRENYQ NGKNYAHEGL
     KKSYSTDIHL WHNGKWDKSG ELSQGRAYGV SLPWNNSLLI IGGETAGGKA VTDSVLITVK
     DNKVTVQN
 
 
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