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Database: UniProt
Entry: A0A0P9CIL3_9BACL
LinkDB: A0A0P9CIL3_9BACL
Original site: A0A0P9CIL3_9BACL 
ID   A0A0P9CIL3_9BACL        Unreviewed;       372 AA.
AC   A0A0P9CIL3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=UDP-N-acetylglucosamine 2-epimerase (non-hydrolyzing) {ECO:0000256|ARBA:ARBA00038858};
DE            EC=5.1.3.14 {ECO:0000256|ARBA:ARBA00038858};
GN   ORFNames=AN477_15895 {ECO:0000313|EMBL:KPV42862.1};
OS   Alicyclobacillus ferrooxydans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Alicyclobacillus.
OX   NCBI_TaxID=471514 {ECO:0000313|EMBL:KPV42862.1, ECO:0000313|Proteomes:UP000050482};
RN   [1] {ECO:0000313|EMBL:KPV42862.1, ECO:0000313|Proteomes:UP000050482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC-34 {ECO:0000313|EMBL:KPV42862.1,
RC   ECO:0000313|Proteomes:UP000050482};
RA   Hemp J.;
RT   "Draft genome sequence of Alicyclobacillus ferrooxydans DSM 22381.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-
CC         mannosamine; Xref=Rhea:RHEA:17213, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:68623; EC=5.1.3.14;
CC         Evidence={ECO:0000256|ARBA:ARBA00036080};
CC   -!- SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
CC       {ECO:0000256|ARBA:ARBA00038209, ECO:0000256|RuleBase:RU003513}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPV42862.1}.
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DR   EMBL; LJCO01000069; KPV42862.1; -; Genomic_DNA.
DR   RefSeq; WP_054970188.1; NZ_LJCO01000069.1.
DR   AlphaFoldDB; A0A0P9CIL3; -.
DR   STRING; 471514.AN477_15895; -.
DR   PATRIC; fig|471514.4.peg.4865; -.
DR   OrthoDB; 9803238at2; -.
DR   Proteomes; UP000050482; Unassembled WGS sequence.
DR   GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IEA:InterPro.
DR   CDD; cd03786; GTB_UDP-GlcNAc_2-Epimerase; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom.
DR   InterPro; IPR029767; WecB-like.
DR   NCBIfam; TIGR00236; wecB; 1.
DR   PANTHER; PTHR43174; UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE; 1.
DR   PANTHER; PTHR43174:SF2; UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE; 1.
DR   Pfam; PF02350; Epimerase_2; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU003513};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050482}.
FT   DOMAIN          20..358
FT                   /note="UDP-N-acetylglucosamine 2-epimerase"
FT                   /evidence="ECO:0000259|Pfam:PF02350"
SQ   SEQUENCE   372 AA;  41266 MW;  F4B066F766D768A5 CRC64;
     MTVFGTRPEA VKMAPLVKVL EQNPFIESLV CVTAQHREML DQVLEVFNVH PDDDLDIMEP
     SQSLGTITRK ALEGLETVIA QRKPDIVLVH GDTTTTLAAA LAAFYQQVKI GHVEAGLRTY
     DKYSPFPEEM NRQLADVLTD LFFAPTSWAA GNLYREAKPE ENVFITGNTA VDAMATTVRQ
     QYHHEVLDSI PDGTRIVYMT SHRRENLGEP LGNICRAARR LVDAHPDVHL IYPMHLNPSV
     RETAVSVLGG HDRIHLIEPL GVIDNHNFMS RSTLILTDSG GIQEEAPSLG VPVLVMRDTT
     ERPEGVEAGT LRLVGTDEEA IYNNGYELLN DEAVYQDMAG RKNPYGDGHA SERIAEAILY
     HFGMGEKPAT FE
//
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