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Database: UniProt
Entry: A0A1S6J0U7_9FIRM
LinkDB: A0A1S6J0U7_9FIRM
Original site: A0A1S6J0U7_9FIRM 
ID   A0A1S6J0U7_9FIRM        Unreviewed;       349 AA.
AC   A0A1S6J0U7;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=UDP-N-acetylglucosamine 2-epimerase (Non-hydrolyzing) {ECO:0000313|EMBL:AQS60649.1};
GN   ORFNames=B0537_15540 {ECO:0000313|EMBL:AQS60649.1};
OS   Desulforamulus ferrireducens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=1833852 {ECO:0000313|EMBL:AQS60649.1, ECO:0000313|Proteomes:UP000189464};
RN   [1] {ECO:0000313|EMBL:AQS60649.1, ECO:0000313|Proteomes:UP000189464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GSS09 {ECO:0000313|EMBL:AQS60649.1,
RC   ECO:0000313|Proteomes:UP000189464};
RX   PubMed=27153808; DOI=10.1099/ijsem.0.001139;
RA   Yang G., Guo J., Zhuang L., Yuan Y., Zhou S.;
RT   "Desulfotomaculum ferrireducens sp. nov., a moderately thermophilic
RT   sulfate-reducing and dissimilatory Fe(III)-reducing bacterium isolated from
RT   compost.";
RL   Int. J. Syst. Evol. Microbiol. 66:3022-3028(2016).
CC   -!- SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
CC       {ECO:0000256|RuleBase:RU003513}.
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DR   EMBL; CP019698; AQS60649.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S6J0U7; -.
DR   STRING; 1833852.B0537_15540; -.
DR   KEGG; dfg:B0537_15540; -.
DR   Proteomes; UP000189464; Chromosome.
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:SF1; 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|RuleBase:RU003513};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189464}.
FT   DOMAIN          10..343
FT                   /note="UDP-N-acetylglucosamine 2-epimerase"
FT                   /evidence="ECO:0000259|Pfam:PF02350"
SQ   SEQUENCE   349 AA;  38971 MW;  ABB4D7FDFE788DF3 CRC64;
     MAPVSAEISK RGYKEYIIHT GQHFDDNMSK VFFDELNIPQ PNLSLSLGTG SHGKMTALML
     MELEIILQEK KPSGVIIYGD TNSTLAAALA AVKLHIPIAH VEAGPRIYDI NTPEEINRIV
     ADHAAKLRFC PDIVSVQNLA KENILNGVYF TGDVMFDSYL IFSKVAREKS TIINSLNLNT
     NEYALLTIHR PNNTDTEDAL KRVIKVLENA KMKIVFPVHP RTEAAFKRHG LWESLKAINH
     AKVIPAVGYL DILELINNAK IVLTDSGGLQ KEAFFAGKPV LVLFHTTPWP QIQSCGWQKC
     CWDNNGIDVN RVIELISSYM PTNRRPNLFG DGNAASKIVD LLENHGWFK
//
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