NANQ_ECOLI
ID NANQ_ECOLI Reviewed; 154 AA.
AC P45424; Q2M8Z2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=N-acetylneuraminate anomerase NanQ {ECO:0000303|PubMed:33895133};
DE AltName: Full=N-acetylneuraminate openase {ECO:0000303|PubMed:33895133};
GN Name=nanQ {ECO:0000303|PubMed:33895133}; Synonyms=yhcH;
GN OrderedLocusNames=b3221, JW3190;
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=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 [2]
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 [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBCELLULAR
RP LOCATION, DOMAIN, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Opens both the alpha- and beta-forms of N-acetylneuraminate
CC (sialic acid; Neu5Ac) to provide aceneuramate, the preferred substrate
CC for NanA. Has preferential activity on the beta-anomer rather than the
CC alpha-anomer. Accelerates a reaction that is spontaneous at slightly
CC alkaline pH, facilitates the reaction at acidic pH.
CC {ECO:0000269|PubMed:33895133}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-alpha-neuraminate = aceneuramate;
CC Xref=Rhea:RHEA:67736, ChEBI:CHEBI:58770, ChEBI:CHEBI:173083;
CC Evidence={ECO:0000269|PubMed:33895133};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67737;
CC Evidence={ECO:0000269|PubMed:33895133};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67738;
CC Evidence={ECO:0000269|PubMed:33895133};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-beta-neuraminate = aceneuramate;
CC Xref=Rhea:RHEA:67740, ChEBI:CHEBI:58705, ChEBI:CHEBI:173083;
CC Evidence={ECO:0000269|PubMed:33895133};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67741;
CC Evidence={ECO:0000269|PubMed:33895133};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67742;
CC Evidence={ECO:0000269|PubMed:33895133};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:33895133};
CC Note=The Zn(2+) ion may play a catalytic role.
CC {ECO:0000305|PubMed:33895133};
CC -!- ACTIVITY REGULATION: Inhibited by 1,10-phenanthroline.
CC {ECO:0000269|PubMed:33895133}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:33895133}.
CC -!- INDUCTION: Negatively regulated by the transcriptional repressor NanR.
CC Induced by N-acetylneuraminate, via inactivation of NanR.
CC {ECO:0000269|PubMed:23935044}.
CC -!- DOMAIN: A His-tag on the N-terminus blocks activity, while a C-terminal
CC His-tag does not. {ECO:0000269|PubMed:33895133}.
CC -!- DISRUPTION PHENOTYPE: No visible effect on growth on Neu5Ac at pH 7.0
CC and 37 degrees Celsius. Shows slight systematic growth delay at pH 6.0
CC and 20 degrees Celsius. No visible phenotype on glucose.
CC {ECO:0000269|PubMed:33895133}.
CC -!- SIMILARITY: Belongs to the NanQ anomerase family. {ECO:0000305}.
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DR EMBL; U18997; AAA58023.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76253.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77264.1; -; Genomic_DNA.
DR PIR; G65113; G65113.
DR RefSeq; NP_417688.1; NC_000913.3.
DR RefSeq; WP_000979882.1; NZ_STEB01000012.1.
DR AlphaFoldDB; P45424; -.
DR SMR; P45424; -.
DR BioGRID; 4261226; 16.
DR IntAct; P45424; 1.
DR STRING; 511145.b3221; -.
DR jPOST; P45424; -.
DR PaxDb; P45424; -.
DR PRIDE; P45424; -.
DR EnsemblBacteria; AAC76253; AAC76253; b3221.
DR EnsemblBacteria; BAE77264; BAE77264; BAE77264.
DR GeneID; 947750; -.
DR KEGG; ecj:JW3190; -.
DR KEGG; eco:b3221; -.
DR PATRIC; fig|511145.12.peg.3317; -.
DR EchoBASE; EB2665; -.
DR eggNOG; COG2731; Bacteria.
DR HOGENOM; CLU_107139_3_1_6; -.
DR InParanoid; P45424; -.
DR OMA; FIDIQIP; -.
DR PhylomeDB; P45424; -.
DR BioCyc; EcoCyc:G7675-MON; -.
DR BioCyc; MetaCyc:G7675-MON; -.
DR PRO; PR:P45424; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR Gene3D; 2.60.120.370; -; 1.
DR InterPro; IPR004375; NanQ/TabA/YiaL.
DR InterPro; IPR037012; NanQ/TabA/YiaL_sf.
DR PANTHER; PTHR34986; PTHR34986; 1.
DR Pfam; PF04074; DUF386; 1.
DR TIGRFAMs; TIGR00022; TIGR00022; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Zinc.
FT CHAIN 1..154
FT /note="N-acetylneuraminate anomerase NanQ"
FT /id="PRO_0000169485"
SQ SEQUENCE 154 AA; 17038 MW; E0E16E2B5AAB7026 CRC64;
MMMGEVQSLP SAGLHPALQD ALTLALAARP QEKAPGRYEL QGDNIFMNVM TFNTQSPVEK
KAELHEQYID IQLLLNGEER ILFGMAGTAR QCEEFHHEDD YQLCSTIDNE QAIILKPGMF
AVFMPGEPHK PGCVVGEPGE IKKVVVKVKA DLMA
