ID C6WNN8_ACTMD Unreviewed; 390 AA.
AC C6WNN8;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 OrderedLocusNames=Amir_1001 {ECO:0000313|EMBL:ACU34957.1};
OS Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064
OS / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinosynnema.
OX NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34957.1, ECO:0000313|Proteomes:UP000002213};
RN [1] {ECO:0000313|EMBL:ACU34957.1, ECO:0000313|Proteomes:UP000002213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 /
RC NRRL B-12336 / IMRU 3971 / 101 {ECO:0000313|Proteomes:UP000002213};
RX PubMed=21304636; DOI=10.4056/sigs.21137;
RA Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L.,
RA Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., Mavromatis K.,
RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA Detter J.C., Han C., Chain P., Tindall B.J., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL Stand. Genomic Sci. 1:46-53(2009).
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}.
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DR EMBL; CP001630; ACU34957.1; -; Genomic_DNA.
DR RefSeq; WP_012783619.1; NC_013093.1.
DR AlphaFoldDB; C6WNN8; -.
DR STRING; 446462.Amir_1001; -.
DR KEGG; ami:Amir_1001; -.
DR eggNOG; COG0381; Bacteria.
DR HOGENOM; CLU_041674_1_0_11; -.
DR OrthoDB; 9803238at2; -.
DR Proteomes; UP000002213; 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: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:UP000002213}.
FT DOMAIN 26..367
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /evidence="ECO:0000259|Pfam:PF02350"
SQ SEQUENCE 390 AA; 41217 MW; 5F69AE39CD14CCE2 CRC64;
MKEVLLLAGT RPEAVKVAPV ALELACHRGI RPVIVHGGQH ADVVEQALAA FGLVPDEVLD
VPRATGTQAE LLSLLVPEID RVLRRRAPAA VLVQGDTTTA LAGALAAFWR GVPVAHLEAG
LRTGELASPF PEEGTRQMIA RIAALHLAPT DDAACALLGE SLPDGNVVVT GNTVVDAVQR
VAAADLPARD PDLAVLERVL DEHGQRLVLV TVHRRESWGE PLDRVLGAVR GIADRHPDVR
VLLPAHPNPA VRAQVVAALG GHPRIVVTEP LDYPDLVRAL RRSALVLTDS GGIQEEAPSF
GVPVLVLRES TERMAAVDAG CAWLVGTDPT RILAEAGWAL GARLRLPHSR NPFGDGFAAI
RVRKALERLL GIAPVPVLSG APTVPAMRVP
//
