ID A0A167TEA0_9BACI Unreviewed; 350 AA.
AC A0A167TEA0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Aldose 1-epimerase {ECO:0000256|PIRNR:PIRNR005096};
DE EC=5.1.3.3 {ECO:0000256|PIRNR:PIRNR005096};
GN ORFNames=GFC30_2160 {ECO:0000313|EMBL:ANB60344.1};
OS Anoxybacillus amylolyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=294699 {ECO:0000313|EMBL:ANB60344.1, ECO:0000313|Proteomes:UP000076865};
RN [1] {ECO:0000313|EMBL:ANB60344.1, ECO:0000313|Proteomes:UP000076865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15939 {ECO:0000313|EMBL:ANB60344.1,
RC ECO:0000313|Proteomes:UP000076865};
RX PubMed=16682297; DOI=10.1016/j.syapm.2005.10.003;
RA Poli A., Esposito E., Lama L., Orlando P., Nicolaus G., de Appolonia F.,
RA Gambacorta A., Nicolaus B.;
RT "Anoxybacillus amylolyticus sp. nov., a thermophilic amylase producing
RT bacterium isolated from Mount Rittmann (Antarctica).";
RL Syst. Appl. Microbiol. 29:300-307(2006).
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; CP015438; ANB60344.1; -; Genomic_DNA.
DR RefSeq; WP_066325248.1; NZ_CP015438.1.
DR AlphaFoldDB; A0A167TEA0; -.
DR KEGG; aamy:GFC30_2160; -.
DR PATRIC; fig|294699.3.peg.2228; -.
DR OrthoDB; 9779408at2; -.
DR UniPathway; UPA00242; -.
DR Proteomes; UP000076865; 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 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.
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:UP000076865}.
FT ACT_SITE 179
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT ACT_SITE 313
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT BINDING 179..181
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT BINDING 252
FT /ligand="beta-D-galactose"
FT /ligand_id="ChEBI:CHEBI:27667"
FT /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ SEQUENCE 350 AA; 39447 MW; 22CA2E9834558E88 CRC64;
MRIVQEQWTE VDGRPIIAYT FTNDNGMEVT CLNYGCIITK ILAPDKYGNY ENVVLAFNEF
SPYLTNSPYF GAVIGRVAGR IREASFELNG KTYQLHKNEN SNHLHGGQKG FHHVVWKAVE
FSTKEAVGVQ FSYTSPDGEE GYPGNVDVQV TYTLNNQNEF IISYHATSDK DTPITLTNHT
YFNLSGNLKS DILHHRLKIK SNQFLELDHQ FIPTGVLLNV ENTPFDLREG KLLKEGIEAN
HPQIALVGQG YDHPFLLDSR HAEEIVLFEP ESGRTLIIET DEPGVVVYTG NHFPSGMKVN
GMPSRKYLGI CLETQALPDA VHHPHFPSCI LRAGEVYSSM TKYTFRVHQA
//