ID D2PWW3_KRIFD Unreviewed; 403 AA. AC D2PWW3; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 27-MAR-2024, entry version 70. DE RecName: Full=Aldose 1-epimerase {ECO:0000256|ARBA:ARBA00014165, ECO:0000256|PIRNR:PIRNR005096}; DE EC=5.1.3.3 {ECO:0000256|ARBA:ARBA00013185, ECO:0000256|PIRNR:PIRNR005096}; GN OrderedLocusNames=Kfla_6341 {ECO:0000313|EMBL:ADB35343.1}; OS Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399). OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales; OC Kribbellaceae; Kribbella. OX NCBI_TaxID=479435 {ECO:0000313|EMBL:ADB35343.1, ECO:0000313|Proteomes:UP000007967}; RN [1] {ECO:0000313|Proteomes:UP000007967} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17836 / JCM 10339 / NBRC 14399 RC {ECO:0000313|Proteomes:UP000007967}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N., RA Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., RA Pukall R., Klenk H.-P., Eisen J.A.; RT "The complete genome of Kribbella flavida DSM 17836."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADB35343.1, ECO:0000313|Proteomes:UP000007967} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17836 / JCM 10339 / NBRC 14399 RC {ECO:0000313|Proteomes:UP000007967}; RX PubMed=21304701; RA Pukall R., Lapidus A., Glavina Del Rio T., Copeland A., Tice H., RA Cheng J.-F., Lucas S., Chen F., Nolan M., LaButti K., Pati A., Ivanova N., RA Mavrommatis K., Mikhailova N., Pitluck S., Bruce D., Goodwin L., Land M., RA Hauser L., Chang Y.-J., Jeffries C.D., Chen A., Palaniappan K., Chain P., RA Rohde M., Goeker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.-P., Brettin T.; RT "Complete genome sequence of Kribbella flavida type strain (IFO 14399)."; RL Stand. Genomic Sci. 2:186-193(2010). CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-glucose = beta-D-glucose; Xref=Rhea:RHEA:10264, CC ChEBI:CHEBI:15903, ChEBI:CHEBI:17925; EC=5.1.3.3; CC Evidence={ECO:0000256|ARBA:ARBA00001614, CC ECO:0000256|PIRNR:PIRNR005096}; CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism. CC {ECO:0000256|ARBA:ARBA00005028, ECO:0000256|PIRNR:PIRNR005096}. CC -!- SIMILARITY: Belongs to the aldose epimerase family. CC {ECO:0000256|ARBA:ARBA00006206, ECO:0000256|PIRNR:PIRNR005096}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001736; ADB35343.1; -; Genomic_DNA. DR RefSeq; WP_012923896.1; NC_013729.1. DR AlphaFoldDB; D2PWW3; -. DR STRING; 479435.Kfla_6341; -. DR KEGG; kfl:Kfla_6341; -. DR eggNOG; COG2017; Bacteria. DR HOGENOM; CLU_031753_2_0_11; -. DR OrthoDB; 9779408at2; -. DR UniPathway; UPA00242; -. DR Proteomes; UP000007967; Chromosome. DR GO; GO:0004034; F:aldose 1-epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0019318; P:hexose metabolic process; IEA:UniProtKB-UniPathway. DR CDD; cd09019; galactose_mutarotase_like; 1. DR Gene3D; 2.70.98.10; -; 1. DR InterPro; IPR018052; Ald1_epimerase_CS. DR InterPro; IPR015443; Aldose_1-epimerase. DR InterPro; IPR008183; Aldose_1/G6P_1-epimerase. DR InterPro; IPR011013; Gal_mutarotase_sf_dom. DR InterPro; IPR047215; Galactose_mutarotase-like. DR InterPro; IPR014718; GH-type_carb-bd. DR InterPro; IPR006311; TAT_signal. DR PANTHER; PTHR10091:SF50; ALDOSE 1-EPIMERASE; 1. DR PANTHER; PTHR10091; ALDOSE-1-EPIMERASE; 1. DR Pfam; PF01263; Aldose_epim; 1. DR PIRSF; PIRSF005096; GALM; 1. DR SUPFAM; SSF74650; Galactose mutarotase-like; 1. DR PROSITE; PS00545; ALDOSE_1_EPIMERASE; 1. DR PROSITE; PS51318; TAT; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR005096}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PIRNR:PIRNR005096}; KW Reference proteome {ECO:0000313|Proteomes:UP000007967}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..33 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 34..403 FT /note="Aldose 1-epimerase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5003034756" FT ACT_SITE 229 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR005096-1" FT ACT_SITE 368 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR005096-1" FT BINDING 128..129 FT /ligand="beta-D-galactose" FT /ligand_id="ChEBI:CHEBI:27667" FT /evidence="ECO:0000256|PIRSR:PIRSR005096-3" FT BINDING 229..231 FT /ligand="beta-D-galactose" FT /ligand_id="ChEBI:CHEBI:27667" FT /evidence="ECO:0000256|PIRSR:PIRSR005096-3" FT BINDING 301 FT /ligand="beta-D-galactose" FT /ligand_id="ChEBI:CHEBI:27667" FT /evidence="ECO:0000256|PIRSR:PIRSR005096-2" SQ SEQUENCE 403 AA; 43215 MW; 14CCBC1037F32119 CRC64; MPDHLPRRHV LRTAGALGLG AAAAGALTGP ADAAPTATTV ASMGSHHGRL SIRKDPFGTT PEGVGVDVYT FGNGRVTVSM LTWGATIQRV ETPDRRGRTE NISLGFDNLP DYAALSPYFG ATIGRYGNRI AKGRFTLDGR SYQIPVNNGE NALHGGTLGF DKKVWKAKVV QTPSAVGVAF SYVSPDGEMG FPGELTTTVT YTLNKQDDLR IDYHATVAGK PTVVNLTNHV YFNLAGEGSG SIDGHVLQLN APSYTPVDEG LIPTGEIAPV AGTPFDFNRP TAIGARIRDD HPQLVIGRGY DHNFVLGGKP DRDGLRFAAR FWEPEGGRTV TVHTAEPGAQ FYSGNFLDGT FQGIGNKSYR QGDAFAFETQ HFPDSPNHPN FPSTVLRPGE TYRSTTVYSF GTK //