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NANE_STAAN
ID   NANE_STAAN              Reviewed;         222 AA.
AC   P65517; Q99WQ8;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Putative N-acetylmannosamine-6-phosphate 2-epimerase {ECO:0000255|HAMAP-Rule:MF_01235};
DE            EC=5.1.3.9 {ECO:0000255|HAMAP-Rule:MF_01235};
DE   AltName: Full=ManNAc-6-P epimerase {ECO:0000255|HAMAP-Rule:MF_01235};
GN   Name=nanE {ECO:0000255|HAMAP-Rule:MF_01235}; OrderedLocusNames=SA0307;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
CC   -!- FUNCTION: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-
CC       acetylglucosamine-6-phosphate (GlcNAc-6-P). {ECO:0000255|HAMAP-
CC       Rule:MF_01235}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acyl-D-glucosamine 6-phosphate = an N-acyl-D-mannosamine
CC         6-phosphate; Xref=Rhea:RHEA:23932, ChEBI:CHEBI:57599,
CC         ChEBI:CHEBI:57666; EC=5.1.3.9; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01235};
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC       fructose 6-phosphate from N-acetylneuraminate: step 3/5.
CC       {ECO:0000255|HAMAP-Rule:MF_01235}.
CC   -!- SIMILARITY: Belongs to the NanE family. {ECO:0000255|HAMAP-
CC       Rule:MF_01235}.
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DR   EMBL; BA000018; BAB41531.1; -; Genomic_DNA.
DR   PIR; H89796; H89796.
DR   RefSeq; WP_000936718.1; NC_002745.2.
DR   PDB; 1Y0E; X-ray; 1.95 A; A/B=1-222.
DR   PDBsum; 1Y0E; -.
DR   AlphaFoldDB; P65517; -.
DR   SMR; P65517; -.
DR   EnsemblBacteria; BAB41531; BAB41531; BAB41531.
DR   KEGG; sau:SA0307; -.
DR   HOGENOM; CLU_086300_1_0_9; -.
DR   OMA; TRPMEIT; -.
DR   UniPathway; UPA00629; UER00682.
DR   EvolutionaryTrace; P65517; -.
DR   Proteomes; UP000000751; Chromosome.
DR   GO; GO:0047465; F:N-acylglucosamine-6-phosphate 2-epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009385; F:N-acylmannosamine-6-phosphate 2-epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006051; P:N-acetylmannosamine metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04729; NanE; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01235; ManNAc6P_epimer; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR007260; NanE.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   PANTHER; PTHR36204; PTHR36204; 1.
DR   Pfam; PF04131; NanE; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Isomerase.
FT   CHAIN           1..222
FT                   /note="Putative N-acetylmannosamine-6-phosphate 2-
FT                   epimerase"
FT                   /id="PRO_0000179799"
FT   STRAND          4..9
FT                   /evidence="ECO:0007829|PDB:1Y0E"
FT   HELIX           21..34
FT                   /evidence="ECO:0007829|PDB:1Y0E"
FT   STRAND          37..43
FT                   /evidence="ECO:0007829|PDB:1Y0E"
FT   HELIX           44..53
FT                   /evidence="ECO:0007829|PDB:1Y0E"
FT   STRAND          58..61
FT                   /evidence="ECO:0007829|PDB:1Y0E"
FT   HELIX           77..86
FT                   /evidence="ECO:0007829|PDB:1Y0E"
FT   STRAND          89..94
FT                   /evidence="ECO:0007829|PDB:1Y0E"
FT   STRAND          101..103
FT                   /evidence="ECO:0007829|PDB:1Y0E"
FT   HELIX           105..115
FT                   /evidence="ECO:0007829|PDB:1Y0E"
FT   STRAND          119..124
FT                   /evidence="ECO:0007829|PDB:1Y0E"
FT   HELIX           128..136
FT                   /evidence="ECO:0007829|PDB:1Y0E"
FT   STRAND          140..143
FT                   /evidence="ECO:0007829|PDB:1Y0E"
FT   TURN            145..148
FT                   /evidence="ECO:0007829|PDB:1Y0E"
FT   HELIX           160..172
FT                   /evidence="ECO:0007829|PDB:1Y0E"
FT   STRAND          175..182
FT                   /evidence="ECO:0007829|PDB:1Y0E"
FT   HELIX           186..194
FT                   /evidence="ECO:0007829|PDB:1Y0E"
FT   STRAND          198..202
FT                   /evidence="ECO:0007829|PDB:1Y0E"
FT   HELIX           204..207
FT                   /evidence="ECO:0007829|PDB:1Y0E"
FT   HELIX           209..218
FT                   /evidence="ECO:0007829|PDB:1Y0E"
SQ   SEQUENCE   222 AA;  24505 MW;  2977C9D2E628BD2D CRC64;
     MLPHGLIVSC QALADEPLHS SFIMSKMALA AYEGGAVGIR ANTKEDILAI KETVDLPVIG
     IVKRDYDHSD VFITATSKEV DELIESQCEV IALDATLQQR PKETLDELVS YIRTHAPNVE
     IMADIATVEE AKNAARLGFD YIGTTLHGYT SYTQGQLLYQ NDFQFLKDVL QSVDAKVIAE
     GNVITPDMYK RVMDLGVHCS VVGGAITRPK EITKRFVQVM ED
 
 
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