NANQ_HAEIN
ID NANQ_HAEIN Reviewed; 155 AA.
AC P44583;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=N-acetylneuraminate anomerase {ECO:0000303|PubMed:33895133};
DE AltName: Full=N-acetylneuraminate openase {ECO:0000303|PubMed:33895133};
GN Name=nanQ {ECO:0000303|PubMed:33895133}; OrderedLocusNames=HI_0227;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=9719565; DOI=10.1002/elps.1150191046;
RA Fountoulakis M., Juranville J.-F., Roeder D., Evers S., Berndt P.,
RA Langen H.;
RT "Reference map of the low molecular mass proteins of Haemophilus
RT influenzae.";
RL Electrophoresis 19:1819-1827(1998).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=10675023;
RX DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA Fountoulakis M.;
RT "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL Electrophoresis 21:411-429(2000).
RN [4]
RP FUNCTION, AND COFACTOR.
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 [5] {ECO:0007744|PDB:1JOP, ECO:0007744|PDB:1S4C}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH COPPER.
RX PubMed=16077096; DOI=10.1128/jb.187.16.5520-5527.2005;
RA Teplyakov A., Obmolova G., Toedt J., Galperin M.Y., Gilliland G.L.;
RT "Crystal structure of the bacterial YhcH protein indicates a role in sialic
RT acid catabolism.";
RL J. Bacteriol. 187:5520-5527(2005).
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 (Probable). Has preferential activity on the beta-anomer
CC rather than the alpha-anomer. Accelerates a reaction that is
CC spontaneous at slightly alkaline pH, facilitates the reaction at acidic
CC pH (By similarity). {ECO:0000250|UniProtKB:P45424,
CC ECO:0000305|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:0000250|UniProtKB:P45424};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67737;
CC Evidence={ECO:0000250|UniProtKB:P45424};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67738;
CC Evidence={ECO:0000250|UniProtKB:P45424};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-beta-neuraminate = aceneuramate;
CC Xref=Rhea:RHEA:67740, ChEBI:CHEBI:58705, ChEBI:CHEBI:173083;
CC Evidence={ECO:0000250|UniProtKB:P45424};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67741;
CC Evidence={ECO:0000250|UniProtKB:P45424};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67742;
CC Evidence={ECO:0000250|UniProtKB:P45424};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:33895133};
CC Note=Has been crystallized with Cu(2+) but reconstitutes with Zn(2+).
CC {ECO:0000269|PubMed:16077096, ECO:0000269|PubMed:33895133};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P45424}.
CC -!- SIMILARITY: Belongs to the NanQ anomerase family. {ECO:0000305}.
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DR EMBL; L42023; AAC21897.1; -; Genomic_DNA.
DR PIR; F64145; F64145.
DR RefSeq; NP_438399.1; NC_000907.1.
DR RefSeq; WP_005660595.1; NC_000907.1.
DR PDB; 1JOP; X-ray; 2.60 A; A/B/C/D=1-155.
DR PDB; 1S4C; X-ray; 2.20 A; A/B/C/D=1-155.
DR PDBsum; 1JOP; -.
DR PDBsum; 1S4C; -.
DR AlphaFoldDB; P44583; -.
DR SMR; P44583; -.
DR STRING; 71421.HI_0227; -.
DR DNASU; 951142; -.
DR EnsemblBacteria; AAC21897; AAC21897; HI_0227.
DR KEGG; hin:HI_0227; -.
DR PATRIC; fig|71421.8.peg.241; -.
DR eggNOG; COG2731; Bacteria.
DR HOGENOM; CLU_107139_3_1_6; -.
DR OMA; MNVMEFE; -.
DR PhylomeDB; P44583; -.
DR BioCyc; HINF71421:G1GJ1-244-MON; -.
DR EvolutionaryTrace; P44583; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 3D-structure; Copper; Cytoplasm; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..155
FT /note="N-acetylneuraminate anomerase"
FT /id="PRO_0000169486"
FT BINDING 65
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0007744|PDB:1S4C"
FT BINDING 70
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0007744|PDB:1S4C"
FT BINDING 130
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0007744|PDB:1S4C"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:1S4C"
FT TURN 9..14
FT /evidence="ECO:0007829|PDB:1S4C"
FT HELIX 17..26
FT /evidence="ECO:0007829|PDB:1S4C"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:1S4C"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:1S4C"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1S4C"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:1S4C"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:1S4C"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1S4C"
FT STRAND 66..77
FT /evidence="ECO:0007829|PDB:1S4C"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:1S4C"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:1S4C"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:1S4C"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:1S4C"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:1S4C"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:1S4C"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:1S4C"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:1S4C"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:1S4C"
SQ SEQUENCE 155 AA; 17670 MW; DAC9FEEAE69B11C1 CRC64;
MIISSLTNPN FKVGLPKVIA EVCDYLNTLD LNALENGRHD INDQIYMNVM EPETAEPSSK
KAELHHEYLD VQVLIRGTEN IEVGATYPNL SKYEDYNEAD DYQLCADIDD KFTVTMKPKM
FAVFYPYEPH KPCCVVNGKT EKIKKLVVKV PVKLI
