ID   GALM_ACICA              Reviewed;         381 AA.
AC   P05149;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Aldose 1-epimerase;
DE            EC=5.1.3.3 {ECO:0000269|PubMed:3531172};
DE   AltName: Full=Galactose mutarotase;
DE   AltName: Full=Type-1 mutarotase;
DE   Flags: Precursor;
GN   Name=mro {ECO:0000303|PubMed:3531172};
OS   Acinetobacter calcoaceticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX   PubMed=3012466; DOI=10.1093/nar/14.10.4309;
RA   Gatz C., Hillen W.;
RT   "Acinetobacter calcoaceticus encoded mutarotase: nucleotide sequence
RT   analysis of the gene and characterization of its secretion in Escherichia
RT   coli.";
RL   Nucleic Acids Res. 14:4309-4323(1986).
RN   [2]
RP   PROTEIN SEQUENCE OF 21-47, FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=DSM 30007;
RX   PubMed=3531172; DOI=10.1128/jb.168.1.31-39.1986;
RA   Gatz C., Altschmied J., Hillen W.;
RT   "Cloning and expression of the Acinetobacter calcoaceticus mutarotase gene
RT   in Escherichia coli.";
RL   J. Bacteriol. 168:31-39(1986).
CC   -!- FUNCTION: Mutarotase converts alpha-aldose to the beta-anomer. Active
CC       on D-glucose. {ECO:0000269|PubMed:3531172}.
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:0000269|PubMed:3531172};
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:3012466}.
CC   -!- SIMILARITY: Belongs to the aldose epimerase family. {ECO:0000305}.
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DR   EMBL; X03893; CAA27530.1; -; Genomic_DNA.
DR   PIR; A24487; A24487.
DR   PIR; A29277; A29277.
DR   AlphaFoldDB; P05149; -.
DR   SMR; P05149; -.
DR   STRING; 471.BUM88_04655; -.
DR   BioCyc; MetaCyc:MON-6082; -.
DR   UniPathway; UPA00242; -.
DR   GO; GO:0042597; C:periplasmic space; 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; 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; IPR014718; GH-type_carb-bd.
DR   Pfam; PF01263; Aldose_epim; 1.
DR   PIRSF; PIRSF005096; GALM; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
DR   PROSITE; PS00545; ALDOSE_1_EPIMERASE; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Isomerase; Periplasm;
KW   Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:3531172"
FT   CHAIN           21..381
FT                   /note="Aldose 1-epimerase"
FT                   /id="PRO_0000010472"
FT   ACT_SITE        205
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10126"
FT   ACT_SITE        345
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         279
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        27
FT                   /note="S -> P (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   381 AA;  41550 MW;  F6C0C3FFBAF535A6 CRC64;
     MKKLAILGVT VYSFAQLANA ATLNVKSYGT TQNGQKVDLY TMSNNNGVSV SFISFGGVIT
     QILTPDAQGK QNNIVLGFDD LKGYEVTDTK EGIHFGGLIG RYANRIGNAK FSLDGKTYNL
     EKNNGPNSLH SGNPGFDKRV WQVKPLVSKG ETVKASLKLT SPNGDQGFPG KLDVEVIYSL
     SDQNEFKIEY KAKTDQPTVV NLTNHSYFNL SGAGNNPYGV LDHVVQLNAG RILVTDQNSL
     PTGEIASVAG TPFDFRMPKA IVKDIRANNQ QLAYGYGYDQ TWVINQKSQG KLNLAAIVVD
     PKSKRTMQVL TTEPSVQMYT ADHLLGNIVG ANGVLYRQAD ALALETQHFP DSPNQPTFPS
     TRLNPNQTYN SVTVFKFGVQ K