GALM_ARTBC
ID GALM_ARTBC Reviewed; 440 AA.
AC D4AMB9;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Probable aldose 1-epimerase ARB_05372 {ECO:0000305};
DE EC=5.1.3.3 {ECO:0000250|UniProtKB:Q96C23};
DE AltName: Full=Galactose mutarotase {ECO:0000250|UniProtKB:Q96C23};
DE Flags: Precursor;
GN ORFNames=ARB_05372;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
CC -!- FUNCTION: Mutarotase converts alpha-aldose to the beta-anomer. It is
CC active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and
CC lactose (By similarity). {ECO:0000250|UniProtKB:P0A9C3}.
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:0000250|UniProtKB:Q96C23};
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism. {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q96C23}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC -!- SIMILARITY: Belongs to the aldose epimerase family. {ECO:0000305}.
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DR EMBL; ABSU01000003; EFE35330.1; -; Genomic_DNA.
DR RefSeq; XP_003015975.1; XM_003015929.1.
DR AlphaFoldDB; D4AMB9; -.
DR SMR; D4AMB9; -.
DR STRING; 663331.D4AMB9; -.
DR EnsemblFungi; EFE35330; EFE35330; ARB_05372.
DR GeneID; 9523891; -.
DR KEGG; abe:ARB_05372; -.
DR eggNOG; KOG1604; Eukaryota.
DR HOGENOM; CLU_031753_0_0_1; -.
DR OMA; GPAVNWA; -.
DR UniPathway; UPA00242; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 Gene3D; 2.70.98.10; -; 1.
DR InterPro; IPR008183; Aldose_1/G6P_1-epimerase.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR014718; GH-type_carb-bd.
DR Pfam; PF01263; Aldose_epim; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycoprotein; Isomerase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..440
FT /note="Probable aldose 1-epimerase ARB_05372"
FT /id="PRO_5003054258"
FT ACT_SITE 233
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q96C23"
FT ACT_SITE 401
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q96C23"
FT BINDING 125..126
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96C23"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96C23"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 440 AA; 47835 MW; F6E0AD9BDBDA00BF CRC64;
MCGVLRQLML LLLAFLSITP SCSAWNFHHQ LNGTTPSNGT TTNGSSSCPL ANGASSNPLQ
VYTIAANNIT ASFIPYGARL ISLMVPDREG KMQDVIVGYD NPQDYVKDTL TNHTYFGCIV
GRYANRIRNG TFVLDGTTYN TPKNELNKTQ TLHGGSVGYD QRNWTVTALS NSSITFTLFD
SGYEHFPGDV INHVTFSVNS SYGLKRPNPQ TEFTARTVSL SLTEKTPIML SPHIYWNLNA
FKNETVLEDT LLELPLSSRY VEVDSRLIPT GNIGNVSSSL NGTLDFTKGK LIGKDIKSAD
GICGANCTGY DNCFIIDRPN NASDWTSSPQ TMVPAVNMSS ITTGINMLVT TNQQAIQIYS
CNGQNGTIPV KGSQVARNKA SGDGNGTVVD KIEQYGCLVI ETEGWIDGIN NPDWGQDPFQ
IYSPESGPAI NWATYVFTAS
