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Database: UniProt
Entry: A0A0C2JQT1_9ACTN
LinkDB: A0A0C2JQT1_9ACTN
Original site: A0A0C2JQT1_9ACTN 
ID   A0A0C2JQT1_9ACTN        Unreviewed;       330 AA.
AC   A0A0C2JQT1;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Epimerase {ECO:0000313|EMBL:KIH99157.1};
GN   ORFNames=LP52_08410 {ECO:0000313|EMBL:KIH99157.1};
OS   Streptomonospora alba.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Streptomonospora.
OX   NCBI_TaxID=183763 {ECO:0000313|EMBL:KIH99157.1, ECO:0000313|Proteomes:UP000031675};
RN   [1] {ECO:0000313|Proteomes:UP000031675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 90003 {ECO:0000313|Proteomes:UP000031675};
RX   PubMed=25601074; DOI=10.1016/j.chembiol.2014.11.017;
RA   Metelev M., Tietz J.I., Melby J.O., Blair P.M., Zhu L., Livnat I.,
RA   Severinov K., Mitchell D.A.;
RT   "Structure, bioactivity, and resistance mechanism of streptomonomicin, an
RT   unusual lasso Peptide from an understudied halophilic actinomycete.";
RL   Chem. Biol. 22:241-250(2015).
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911};
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:KIH99157.1}.
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DR   EMBL; JROO01000014; KIH99157.1; -; Genomic_DNA.
DR   RefSeq; WP_040272225.1; NZ_JROO01000014.1.
DR   AlphaFoldDB; A0A0C2JQT1; -.
DR   STRING; 183763.LP52_08410; -.
DR   Proteomes; UP000031675; Unassembled WGS sequence.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0048040; F:UDP-glucuronate decarboxylase activity; IEA:InterPro.
DR   GO; GO:0042732; P:D-xylose metabolic process; IEA:InterPro.
DR   CDD; cd05230; UGD_SDR_e; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR044516; UXS.
DR   PANTHER; PTHR43078:SF6; UDP-GLUCURONIC ACID DECARBOXYLASE 1; 1.
DR   PANTHER; PTHR43078; UDP-GLUCURONIC ACID DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031675}.
FT   DOMAIN          10..244
FT                   /note="NAD-dependent epimerase/dehydratase"
FT                   /evidence="ECO:0000259|Pfam:PF01370"
SQ   SEQUENCE   330 AA;  35397 MW;  B8F035B7917F6491 CRC64;
     MSQAAIGRAV VTGGAGFVGS HLCGHLLDAG AEVVCIDNFA TGSAENVRHL AGRTGFRTLE
     ADVTHPLHVP GRVDTVFHLA SAASPRDYLR LPVETLEAGS RGTRNVLDLA AEHGARTVLA
     STSEVYGDPL HHPQHESYWG NVNPVGPRSV YDEAKRYAEA LTMAYHRAHG ADVGIARIFN
     SYGPGMRPDD GRAIPTFIRQ ALAGEPITVC GDGMQTRSVC YVDDTVRGLI ALAAADITGP
     VNIGSQHELS MHALAELVRA VCGSDSPVVH VGRPQDDPRF RRPDIALAAR ALGWWPLVPM
     EEGLRRTVEW FARARTEPED RSAEPTAGRA
//
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