NANE_CALS4
ID NANE_CALS4 Reviewed; 237 AA.
AC Q8R7I7;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 2.
DT 25-MAY-2022, entry version 103.
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=TTE2420;
OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Caldanaerobacter.
OX NCBI_TaxID=273068;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX PubMed=11997336; DOI=10.1101/gr.219302;
RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA Wang J., Yu J., Yang H.;
RT "A complete sequence of the T. tengcongensis genome.";
RL Genome Res. 12:689-700(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM25556.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE008691; AAM25556.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q8R7I7; -.
DR SMR; Q8R7I7; -.
DR STRING; 273068.TTE2420; -.
DR EnsemblBacteria; AAM25556; AAM25556; TTE2420.
DR KEGG; tte:TTE2420; -.
DR eggNOG; COG3010; Bacteria.
DR HOGENOM; CLU_086300_1_0_9; -.
DR OMA; TRPMEIT; -.
DR UniPathway; UPA00629; UER00682.
DR Proteomes; UP000000555; 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 3: Inferred from homology;
KW Carbohydrate metabolism; Isomerase; Reference proteome.
FT CHAIN 1..237
FT /note="Putative N-acetylmannosamine-6-phosphate 2-
FT epimerase"
FT /id="PRO_0000179816"
SQ SEQUENCE 237 AA; 26268 MW; 57466D47029064E0 CRC64;
MQMDIIQKLE NGLIVSCQAL EGEPLHSPFI MAKMAKAAEI GGAVAIRANG YEDIVAIKKE
VSIPVIGLIK KRYEGYAPYI TPTMEEVDKV IEAGADIVAI DATKAYKPGG LTTGEFLKRI
KEKYPKILVM ADISTYEEGI EAEKLGFDLI STTLSGYTEY SPELEGPDYE LIERLARKVN
VPIIAEGRIW TPEEAVKALE KGAYAVVVGT AITRPHEITR RFVTFIKERR YSNVRAK
