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Database: UniProt
Entry: D2R810_PIRSD
LinkDB: D2R810_PIRSD
Original site: D2R810_PIRSD 
ID   D2R810_PIRSD            Unreviewed;       322 AA.
AC   D2R810;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=NAD-dependent epimerase/dehydratase {ECO:0000313|EMBL:ADB19341.1};
GN   OrderedLocusNames=Psta_4699 {ECO:0000313|EMBL:ADB19341.1};
OS   Pirellula staleyi (strain ATCC 27377 / DSM 6068 / ICPB 4128) (Pirella
OS   staleyi).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Pirellula.
OX   NCBI_TaxID=530564 {ECO:0000313|EMBL:ADB19341.1, ECO:0000313|Proteomes:UP000001887};
RN   [1] {ECO:0000313|EMBL:ADB19341.1, ECO:0000313|Proteomes:UP000001887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27377 / DSM 6068 / ICPB 4128
RC   {ECO:0000313|Proteomes:UP000001887};
RX   PubMed=21304671; DOI=10.4056/sigs.51657;
RA   Clum A., Tindall B.J., Sikorski J., Ivanova N., Mavrommatis K., Lucas S.,
RA   Glavina del Rio T., Nolan M., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA   Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA   Goodwin L., Ovchinikova G., Pati A., Mikhailova N., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Pirellula staleyi type strain (ATCC 27377).";
RL   Stand. Genomic Sci. 1:308-316(2009).
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911};
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DR   EMBL; CP001848; ADB19341.1; -; Genomic_DNA.
DR   RefSeq; WP_012913600.1; NC_013720.1.
DR   AlphaFoldDB; D2R810; -.
DR   STRING; 530564.Psta_4699; -.
DR   KEGG; psl:Psta_4699; -.
DR   eggNOG; COG0451; Bacteria.
DR   HOGENOM; CLU_007383_4_0_0; -.
DR   OrthoDB; 258549at2; -.
DR   UniPathway; UPA00796; UER00771.
DR   Proteomes; UP000001887; Chromosome.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0048040; F:UDP-glucuronate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042732; P:D-xylose metabolic process; IEA:InterPro.
DR   GO; GO:0033320; P:UDP-D-xylose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05230; UGD_SDR_e; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000001887}.
FT   DOMAIN          5..232
FT                   /note="NAD-dependent epimerase/dehydratase"
FT                   /evidence="ECO:0000259|Pfam:PF01370"
SQ   SEQUENCE   322 AA;  36315 MW;  1D981C1967FFC0FE CRC64;
     MIKRILVTGG AGFLGSHLCE RLVDLGHDVV CLDNFFTSQK TNVAHLLGRP NFDLIRHDIT
     SPIWLEVDEI YNLACPAAPG HYQFNPIKTM KTSVLGMINM LGMARRCKAK VLQASTSEVY
     GDPEVHPQVE SYRGNVNPIG IRACYDEGKR AAETLMMDYH RSNGINIRIV RIFNTYGPRM
     HPFDGRVVSN FIRQALTGED LTIFGNGDQT RSFCFRDDLV EGLIRMMHAS DSFTGPCNLG
     NPDEFTVREL AELVLELTGS KSKIVSLPLP ADDPVRRRPD ITLAKTNLDW QPMVPLKEGL
     RRTIEWFRSV NISHYRPPTP NF
//
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