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Database: UniProt
Entry: U1Q2P7_9ACTO
LinkDB: U1Q2P7_9ACTO
Original site: U1Q2P7_9ACTO 
ID   U1Q2P7_9ACTO            Unreviewed;       402 AA.
AC   U1Q2P7;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=HMPREF0043_01711 {ECO:0000313|EMBL:ERH16826.1};
OS   Actinobaculum sp. oral taxon 183 str. F0552.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinobaculum.
OX   NCBI_TaxID=1227261 {ECO:0000313|EMBL:ERH16826.1, ECO:0000313|Proteomes:UP000016495};
RN   [1] {ECO:0000313|EMBL:ERH16826.1, ECO:0000313|Proteomes:UP000016495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0552 {ECO:0000313|EMBL:ERH16826.1,
RC   ECO:0000313|Proteomes:UP000016495};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA   Wilson R.K.;
RL   Submitted (JUN-2013) 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:ERH16826.1}.
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DR   EMBL; AWSB01000051; ERH16826.1; -; Genomic_DNA.
DR   AlphaFoldDB; U1Q2P7; -.
DR   STRING; 1227261.HMPREF0043_01711; -.
DR   PATRIC; fig|1227261.3.peg.1510; -.
DR   eggNOG; COG0381; Bacteria.
DR   HOGENOM; CLU_041674_1_0_11; -.
DR   OrthoDB; 9803238at2; -.
DR   Proteomes; UP000016495; 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:UP000016495}.
FT   DOMAIN          28..370
FT                   /note="UDP-N-acetylglucosamine 2-epimerase"
FT                   /evidence="ECO:0000259|Pfam:PF02350"
SQ   SEQUENCE   402 AA;  43783 MW;  10ACC6D2D7DE5D51 CRC64;
     MPSTAAIRVM LVYGTRPEAI KMAPLVKAFA QDPRFDPRIV VTGQHREMLD QVHSFFDIKP
     DLDLNIHKPG QTLTQVTTRT LQGTDEAIRG FAPDAIAVQG DTSSAFAAAL AAFYHQKPVL
     HVEAGLRTGD IASPFPEEAN RRLIGQLTAL HLCPTAESKD NLLRENTPPE SIRVTGNTVI
     DALLAAVERP VPSGDERLDA AVAETSRRMV LVTAHRRESW GAPMARIGRA VARLADAFPD
     VVFALPAHRN PQVREALLPV LEGRANVVVT EPLEYGAICT VMNRSDLVLT DSGGIQEEAP
     ALSKPVLVLR ENTERPEAVE HGVARVVGTD ENRIVEEASI LLSRDDEYAK MAHAANPYGD
     GRACERILAA TASLFGRGEP LSDFVPHRQR ERDVTSENHA IV
//
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