位置:首页 > 蛋白库 > NANA_STAA1
NANA_STAA1
ID   NANA_STAA1              Reviewed;         293 AA.
AC   A7WXZ2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=N-acetylneuraminate lyase {ECO:0000255|HAMAP-Rule:MF_01237};
DE            Short=NAL {ECO:0000255|HAMAP-Rule:MF_01237};
DE            Short=Neu5Ac lyase {ECO:0000255|HAMAP-Rule:MF_01237};
DE            EC=4.1.3.3 {ECO:0000255|HAMAP-Rule:MF_01237};
DE   AltName: Full=N-acetylneuraminate pyruvate-lyase {ECO:0000255|HAMAP-Rule:MF_01237};
DE   AltName: Full=N-acetylneuraminic acid aldolase {ECO:0000255|HAMAP-Rule:MF_01237};
DE   AltName: Full=Sialate lyase {ECO:0000255|HAMAP-Rule:MF_01237};
DE   AltName: Full=Sialic acid aldolase {ECO:0000255|HAMAP-Rule:MF_01237};
DE   AltName: Full=Sialic acid lyase {ECO:0000255|HAMAP-Rule:MF_01237};
GN   Name=nanA {ECO:0000255|HAMAP-Rule:MF_01237}; OrderedLocusNames=SAHV_0312;
OS   Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=418127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu3 / ATCC 700698;
RX   PubMed=17954695; DOI=10.1128/aac.00534-07;
RA   Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT   "Mutated response regulator graR is responsible for phenotypic conversion
RT   of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT   resistance to vancomycin-intermediate resistance.";
RL   Antimicrob. Agents Chemother. 52:45-53(2008).
CC   -!- FUNCTION: Catalyzes the reversible aldol cleavage of N-acetylneuraminic
CC       acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine
CC       (ManNAc) via a Schiff base intermediate. {ECO:0000255|HAMAP-
CC       Rule:MF_01237}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aceneuramate = N-acetyl-D-mannosamine + pyruvate;
CC         Xref=Rhea:RHEA:23296, ChEBI:CHEBI:15361, ChEBI:CHEBI:17122,
CC         ChEBI:CHEBI:173083; EC=4.1.3.3; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01237};
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC       fructose 6-phosphate from N-acetylneuraminate: step 1/5.
CC       {ECO:0000255|HAMAP-Rule:MF_01237}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01237}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01237}.
CC   -!- SIMILARITY: Belongs to the DapA family. NanA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01237}.
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; AP009324; BAF77195.1; -; Genomic_DNA.
DR   RefSeq; WP_001030736.1; NC_009782.1.
DR   AlphaFoldDB; A7WXZ2; -.
DR   SMR; A7WXZ2; -.
DR   KEGG; saw:SAHV_0312; -.
DR   HOGENOM; CLU_049343_5_1_9; -.
DR   OMA; VVPPVCT; -.
DR   UniPathway; UPA00629; UER00680.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008747; F:N-acetylneuraminate lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00954; NAL; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01237; N_acetylneuram_lyase; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002220; DapA-like.
DR   InterPro; IPR005264; NanA.
DR   InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR   Pfam; PF00701; DHDPS; 1.
DR   PIRSF; PIRSF001365; DHDPS; 1.
DR   PRINTS; PR00146; DHPICSNTHASE.
DR   SMART; SM01130; DHDPS; 1.
DR   PROSITE; PS00666; DHDPS_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Lyase; Schiff base.
FT   CHAIN           1..293
FT                   /note="N-acetylneuraminate lyase"
FT                   /id="PRO_1000066936"
FT   ACT_SITE        165
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
FT   BINDING         48..49
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
FT   SITE            137
FT                   /note="Involved in proton transfer during cleavage"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01237"
SQ   SEQUENCE   293 AA;  33101 MW;  4D07DEFFDC1AF701 CRC64;
     MNKDLKGLYA ALLVPFDENG QVNEQGLKQI AQNAIETEEL DGLYVNGSSG ENFLLNTEQK
     KQVFKVAKEA VGDKVKLIAQ VGSLDLNEAI ELGKYATELG YDALSAVTPF YYPFTFEEIR
     DYYFDIIEAT QNNMIIYAIP DLTGVNISIE QFSELFNHEK IVGVKYTAPN FFLLERIRKA
     FPDKLILSGF DEMLVQATIS GVDGAIGSTY NVNGRRARKI FDLARQGQIQ EAYQLQHDSN
     DIIETVLSMG IYPTLKEILR HRDIDAGLPK RPFKPFNEAH RQTLDQLIAK YDL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024