ID A0A0S9C8F1_9SPHN Unreviewed; 364 AA.
AC A0A0S9C8F1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=ASE95_16955 {ECO:0000313|EMBL:KQN89886.1};
OS Sphingomonas sp. Leaf231.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736301 {ECO:0000313|EMBL:KQN89886.1, ECO:0000313|Proteomes:UP000051427};
RN [1] {ECO:0000313|EMBL:KQN89886.1, ECO:0000313|Proteomes:UP000051427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf231 {ECO:0000313|EMBL:KQN89886.1,
RC ECO:0000313|Proteomes:UP000051427};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN89886.1, ECO:0000313|Proteomes:UP000051427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf231 {ECO:0000313|EMBL:KQN89886.1,
RC ECO:0000313|Proteomes:UP000051427};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQN89886.1}.
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DR EMBL; LMLS01000006; KQN89886.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S9C8F1; -.
DR STRING; 1736301.ASE95_16955; -.
DR OrthoDB; 9803238at2; -.
DR Proteomes; UP000051427; 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:UP000051427}.
FT DOMAIN 18..363
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /evidence="ECO:0000259|Pfam:PF02350"
SQ SEQUENCE 364 AA; 39171 MW; A1DE9F9EB68ADCDA CRC64;
MVVFGTRPEA IKLFPVVRAL AERPGIQIRT CVTAQHRGLL DQVLDVAGIV PDHDLNIMEP
NQSLDRLLAR LVTGVGGVLD VEPIDRVIVQ GDTATALAGA LASYYRKIPV AHVEAGLRSG
DIYHPWPEEV NRRMIAPIAD YHFAPTETAA EALRREGITH GVHVTGNTVI DALHATLARI
ADTPSMTRAL DAIRPRIAER KVVLVTTHRR ENFGDGMQQI ASAIARIAQR DDVAVLFPVH
PNPSVVSVMD AMLGGCDNVI RVDPLDYPTF VSALSLSHIV LTDSGGVQEE APALGKPVLV
MRETTERPEG VAAGTARLVG ARTDQIVAGV MDLLDHPETY LAMSRAHNPF GDGKSAARIA
DLLS
//
