ID K4R249_STRDJ Unreviewed; 381 AA.
AC K4R249;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Aldose 1-epimerase {ECO:0000256|PIRNR:PIRNR005096};
DE EC=5.1.3.3 {ECO:0000256|PIRNR:PIRNR005096};
GN Name=mro {ECO:0000313|EMBL:CCK30321.1};
GN ORFNames=BN159_5942 {ECO:0000313|EMBL:CCK30321.1};
OS Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1214101 {ECO:0000313|EMBL:CCK30321.1, ECO:0000313|Proteomes:UP000008043};
RN [1] {ECO:0000313|EMBL:CCK30321.1, ECO:0000313|Proteomes:UP000008043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 101723 / JCM 4913 / KCC S-0913 / 768
RC {ECO:0000313|Proteomes:UP000008043};
RX PubMed=23043000; DOI=10.1128/JB.01592-12;
RA Jankowitsch F., Schwarz J., Ruckert C., Gust B., Szczepanowski R., Blom J.,
RA Pelzer S., Kalinowski J., Mack M.;
RT "Genome sequence of the bacterium Streptomyces davawensis JCM 4913 and
RT heterologous production of the unique antibiotic roseoflavin.";
RL J. Bacteriol. 194:6818-6827(2012).
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|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}.
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DR EMBL; HE971709; CCK30321.1; -; Genomic_DNA.
DR RefSeq; WP_015660657.1; NC_020504.1.
DR AlphaFoldDB; K4R249; -.
DR STRING; 1214101.BN159_5942; -.
DR KEGG; sdv:BN159_5942; -.
DR PATRIC; fig|1214101.3.peg.6025; -.
DR eggNOG; COG2017; Bacteria.
DR HOGENOM; CLU_031753_2_0_11; -.
DR OrthoDB; 9779408at2; -.
DR UniPathway; UPA00242; -.
DR Proteomes; UP000008043; 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; 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; 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:UP000008043};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..381
FT /note="Aldose 1-epimerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003879781"
FT REGION 350..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 209
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT ACT_SITE 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT BINDING 109..110
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT BINDING 209..211
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT BINDING 281
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ SEQUENCE 381 AA; 41344 MW; 98A34637E900BD14 CRC64;
MELNRRTLIA GAAAAGVTAA MSGTAHATGG HRPVKSLFGK LADGTKIYSW SLENGGTRLK
VLSYGGIVQS LEIPDRRGRY TNVSLGFDNI EDYVASSPYF GALIGRFGNR IGKGKFTLDG
KDYQLSVNDG ENSLHGGSKG FDKVVWDIEP FTKGSDVGLY LYYTSVDGEM GYPGTLRTKV
TYTLTRSGDW RIDYEATTDK ATVVNLTSHV YWNLAGESSG TIYDHELSIA ASRYTPVDSG
LIPTGELAKV AGTPFDFRRT KTVGEDIRVA HQQLLYGKGI DHNWVLDKGS TSRPQWVATL
RDPSSGRTLK IATTEPGLQF YSGNFLDGTL VGSGGSIYRQ GDALCLETQH FPDSPNQPSF
PSTTLRPGQT YRTTTVHSFS A
//
