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NANE2_SALTY
ID   NANE2_SALTY             Reviewed;         229 AA.
AC   Q8ZLQ7;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Putative N-acetylmannosamine-6-phosphate 2-epimerase 2;
DE            EC=5.1.3.9;
DE   AltName: Full=ManNAc-6-P epimerase 2;
GN   Name=nanE2; OrderedLocusNames=STM3337;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-
CC       acetylglucosamine-6-phosphate (GlcNAc-6-P). {ECO:0000305}.
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;
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC       fructose 6-phosphate from N-acetylneuraminate: step 3/5.
CC   -!- SIMILARITY: Belongs to the NanE family. {ECO:0000305}.
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DR   EMBL; AE006468; AAL22206.1; -; Genomic_DNA.
DR   RefSeq; NP_462247.1; NC_003197.2.
DR   RefSeq; WP_000054441.1; NC_003197.2.
DR   PDB; 3IGS; X-ray; 1.50 A; A/B=1-229.
DR   PDBsum; 3IGS; -.
DR   AlphaFoldDB; Q8ZLQ7; -.
DR   SMR; Q8ZLQ7; -.
DR   STRING; 99287.STM3337; -.
DR   PaxDb; Q8ZLQ7; -.
DR   EnsemblBacteria; AAL22206; AAL22206; STM3337.
DR   GeneID; 1254860; -.
DR   KEGG; stm:STM3337; -.
DR   PATRIC; fig|99287.12.peg.3538; -.
DR   HOGENOM; CLU_086300_0_0_6; -.
DR   OMA; TRPMEIT; -.
DR   PhylomeDB; Q8ZLQ7; -.
DR   BioCyc; SENT99287:STM3337-MON; -.
DR   UniPathway; UPA00629; UER00682.
DR   EvolutionaryTrace; Q8ZLQ7; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0006053; P:N-acetylmannosamine catabolic process; IBA:GO_Central.
DR   GO; GO:0019262; P:N-acetylneuraminate catabolic process; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..229
FT                   /note="Putative N-acetylmannosamine-6-phosphate 2-epimerase
FT                   2"
FT                   /id="PRO_0000179795"
FT   HELIX           3..14
FT                   /evidence="ECO:0007829|PDB:3IGS"
FT   STRAND          17..20
FT                   /evidence="ECO:0007829|PDB:3IGS"
FT   HELIX           32..44
FT                   /evidence="ECO:0007829|PDB:3IGS"
FT   STRAND          48..54
FT                   /evidence="ECO:0007829|PDB:3IGS"
FT   HELIX           55..62
FT                   /evidence="ECO:0007829|PDB:3IGS"
FT   STRAND          69..72
FT                   /evidence="ECO:0007829|PDB:3IGS"
FT   HELIX           88..97
FT                   /evidence="ECO:0007829|PDB:3IGS"
FT   STRAND          100..105
FT                   /evidence="ECO:0007829|PDB:3IGS"
FT   HELIX           115..124
FT                   /evidence="ECO:0007829|PDB:3IGS"
FT   STRAND          128..132
FT                   /evidence="ECO:0007829|PDB:3IGS"
FT   HELIX           136..144
FT                   /evidence="ECO:0007829|PDB:3IGS"
FT   STRAND          148..151
FT                   /evidence="ECO:0007829|PDB:3IGS"
FT   TURN            153..156
FT                   /evidence="ECO:0007829|PDB:3IGS"
FT   STRAND          157..161
FT                   /evidence="ECO:0007829|PDB:3IGS"
FT   HELIX           168..176
FT                   /evidence="ECO:0007829|PDB:3IGS"
FT   STRAND          181..185
FT                   /evidence="ECO:0007829|PDB:3IGS"
FT   HELIX           190..198
FT                   /evidence="ECO:0007829|PDB:3IGS"
FT   STRAND          202..206
FT                   /evidence="ECO:0007829|PDB:3IGS"
FT   HELIX           208..211
FT                   /evidence="ECO:0007829|PDB:3IGS"
FT   HELIX           213..228
FT                   /evidence="ECO:0007829|PDB:3IGS"
SQ   SEQUENCE   229 AA;  24030 MW;  77FC1C3BE0B70719 CRC64;
     MSLLEQLDKN IAASGGLIVS CQPVPGSPLD KPEIVAAMAL AAEQAGAVAV RIEGIDNLRM
     TRSLVSVPII GIIKRDLDES PVRITPFLDD VDALAQAGAA IIAVDGTARQ RPVAVEALLA
     RIHHHHLLAM ADCSSVDDGL ACQRLGADII GTTMSGYTTP DTPEEPDLPL VKALHDAGCR
     VIAEGRYNSP ALAAEAIRYG AWAVTVGSAI TRLEHICGWY NDALKKAAS
 
 
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