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Database: UniProt
Entry: T2KQT8_FORAG
LinkDB: T2KQT8_FORAG
Original site: T2KQT8_FORAG 
ID   T2KQT8_FORAG            Unreviewed;       361 AA.
AC   T2KQT8;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=UDP-N-acetylglucosamine 2-epimerase {ECO:0000313|EMBL:CDF81212.1};
DE            EC=5.1.3.14 {ECO:0000313|EMBL:CDF81212.1};
GN   ORFNames=BN863_35000 {ECO:0000313|EMBL:CDF81212.1};
OS   Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 /
OS   M-2Alg 35-1).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Formosa.
OX   NCBI_TaxID=1347342 {ECO:0000313|EMBL:CDF81212.1, ECO:0000313|Proteomes:UP000016160};
RN   [1] {ECO:0000313|EMBL:CDF81212.1, ECO:0000313|Proteomes:UP000016160}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901
RC   {ECO:0000313|Proteomes:UP000016160};
RX   PubMed=23995932; DOI=10.1128/AEM.01937-13;
RA   Mann A.J., Hahnke R.L., Huang S., Werner J., Xing P., Barbeyron T.,
RA   Huettel B., Stueber K., Reinhardt R., Harder J., Gloeckner F.O.,
RA   Amann R.I., Teeling H.;
RT   "The genome of the alga-associated marine flavobacterium Formosa agariphila
RT   KMM 3901T reveals a broad potential for degradation of algal
RT   polysaccharides.";
RL   Appl. Environ. Microbiol. 79:6813-6822(2013).
CC   -!- SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
CC       {ECO:0000256|RuleBase:RU003513}.
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DR   EMBL; HG315671; CDF81212.1; -; Genomic_DNA.
DR   RefSeq; WP_038532788.1; NZ_HG315671.1.
DR   AlphaFoldDB; T2KQT8; -.
DR   STRING; 1347342.BN863_35000; -.
DR   PATRIC; fig|1347342.6.peg.3531; -.
DR   eggNOG; COG0381; Bacteria.
DR   HOGENOM; CLU_041674_0_1_10; -.
DR   OrthoDB; 9803238at2; -.
DR   Proteomes; UP000016160; Chromosome.
DR   GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:CDF81212.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016160}.
FT   DOMAIN          32..358
FT                   /note="UDP-N-acetylglucosamine 2-epimerase"
FT                   /evidence="ECO:0000259|Pfam:PF02350"
SQ   SEQUENCE   361 AA;  40682 MW;  1CFEB40ADA70572D CRC64;
     MKITIVAGAR PNFMKIAPII DAINFKKNEG IDIDFRLVHT GQHYDKNLSD TFFEELNIPY
     PDANLNIKSG TQAEQTAGIM IGFEKELNDN PCDLVLVVGD VTSTMACTIV AKKAGIKVAH
     VEAGIRSGDM NMPEEINRIV TDSLTDYFFT TSEYANENLK NLGVPKNKIY YVGNVMIDTL
     RKHENRLKQP KVWTSIGLKH KSYFVLTLHR PSNVDETESL KELITKIVTL SNNKPIVFPV
     HPRTKKMLSD LNLNFDNLHF IEPLGYLEFN FLVKNAFAVL TDSGGITEET TVMHVPCITL
     RENTERPETC DIGTNYLAGN NPKKLETGFK KLLSNEWPVG EIPKFWDGNT ANRIVNHLLE
     I
//
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