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NANE_FUSNN
ID   NANE_FUSNN              Reviewed;         224 AA.
AC   Q8RDN5;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=FN1476;
OS   Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS   BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX   NCBI_TaxID=190304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC   2640 / LMG 13131 / VPI 4355;
RX   PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA   Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA   Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA   Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA   Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA   Overbeek R.;
RT   "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT   strain ATCC 25586.";
RL   J. Bacteriol. 184:2005-2018(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}.
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DR   EMBL; AE009951; AAL95669.1; -; Genomic_DNA.
DR   RefSeq; NP_604370.1; NC_003454.1.
DR   PDB; 5ZKN; X-ray; 2.21 A; A=1-224.
DR   PDBsum; 5ZKN; -.
DR   AlphaFoldDB; Q8RDN5; -.
DR   SMR; Q8RDN5; -.
DR   STRING; 190304.FN1476; -.
DR   EnsemblBacteria; AAL95669; AAL95669; FN1476.
DR   KEGG; fnu:FN1476; -.
DR   PATRIC; fig|190304.8.peg.2036; -.
DR   eggNOG; COG3010; Bacteria.
DR   HOGENOM; CLU_086300_1_0_0; -.
DR   InParanoid; Q8RDN5; -.
DR   OMA; TRPMEIT; -.
DR   BioCyc; FNUC190304:G1FZS-2044-MON; -.
DR   UniPathway; UPA00629; UER00682.
DR   Proteomes; UP000002521; 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..224
FT                   /note="Putative N-acetylmannosamine-6-phosphate 2-
FT                   epimerase"
FT                   /id="PRO_0000179774"
FT   HELIX           1..6
FT                   /evidence="ECO:0007829|PDB:5ZKN"
FT   TURN            7..10
FT                   /evidence="ECO:0007829|PDB:5ZKN"
FT   STRAND          12..16
FT                   /evidence="ECO:0007829|PDB:5ZKN"
FT   HELIX           27..40
FT                   /evidence="ECO:0007829|PDB:5ZKN"
FT   STRAND          44..49
FT                   /evidence="ECO:0007829|PDB:5ZKN"
FT   HELIX           50..59
FT                   /evidence="ECO:0007829|PDB:5ZKN"
FT   STRAND          64..67
FT                   /evidence="ECO:0007829|PDB:5ZKN"
FT   HELIX           83..92
FT                   /evidence="ECO:0007829|PDB:5ZKN"
FT   STRAND          95..100
FT                   /evidence="ECO:0007829|PDB:5ZKN"
FT   STRAND          102..104
FT                   /evidence="ECO:0007829|PDB:5ZKN"
FT   HELIX           112..122
FT                   /evidence="ECO:0007829|PDB:5ZKN"
FT   STRAND          127..131
FT                   /evidence="ECO:0007829|PDB:5ZKN"
FT   HELIX           135..143
FT                   /evidence="ECO:0007829|PDB:5ZKN"
FT   STRAND          147..150
FT                   /evidence="ECO:0007829|PDB:5ZKN"
FT   TURN            152..155
FT                   /evidence="ECO:0007829|PDB:5ZKN"
FT   HELIX           158..160
FT                   /evidence="ECO:0007829|PDB:5ZKN"
FT   HELIX           165..175
FT                   /evidence="ECO:0007829|PDB:5ZKN"
FT   STRAND          180..185
FT                   /evidence="ECO:0007829|PDB:5ZKN"
FT   HELIX           189..198
FT                   /evidence="ECO:0007829|PDB:5ZKN"
FT   STRAND          201..205
FT                   /evidence="ECO:0007829|PDB:5ZKN"
FT   HELIX           207..210
FT                   /evidence="ECO:0007829|PDB:5ZKN"
FT   HELIX           212..222
FT                   /evidence="ECO:0007829|PDB:5ZKN"
SQ   SEQUENCE   224 AA;  24823 MW;  9F47DE55E8924593 CRC64;
     MNKILESIRG KLIVSCQALE DEPLHSSFIM GRMAYAAYSG GAAGIRANTV EDIKEIKKNV
     SLPIIGIIKK VYNNSDVYIT PTIKEVEDLI NEGVQIIAID ATKRERPDRK DLKNFIAEIK
     EKYPNQLFMA DISSVDEALY AEKIGFDIVG TTLVGYTDYT KNYKALEELK KVVKVVKIPV
     IAEGNIDTPL KAKKALEIGA FAVVVGGAIT RPQQITKKFV DEMK
 
 
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