ID   GALM_HAEIN              Reviewed;         340 AA.
AC   P31765;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Aldose 1-epimerase;
DE            EC=5.1.3.3;
DE   AltName: Full=Galactose mutarotase;
DE   AltName: Full=Type-1 mutarotase;
GN   Name=galM; Synonyms=mro; OrderedLocusNames=HI_0818;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-116.
RC   STRAIN=RM 7004 / Serotype B;
RX   PubMed=1282642; DOI=10.1111/j.1365-2958.1992.tb01763.x;
RA   Maskell D.J., Szabo M.J., Deadman M.E., Moxon E.R.;
RT   "The gal locus from Haemophilus influenzae: cloning, sequencing and the use
RT   of gal mutants to study lipopolysaccharide.";
RL   Mol. Microbiol. 6:3051-3063(1992).
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}.
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:0000255|PROSITE-ProRule:PRU10126};
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the aldose epimerase family. {ECO:0000305}.
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; L42023; AAC22477.1; -; Genomic_DNA.
DR   EMBL; X65934; CAA46732.1; -; Genomic_DNA.
DR   PIR; C64096; C64096.
DR   RefSeq; NP_438978.1; NC_000907.1.
DR   RefSeq; WP_005693182.1; NC_000907.1.
DR   AlphaFoldDB; P31765; -.
DR   SMR; P31765; -.
DR   STRING; 71421.HI_0818; -.
DR   EnsemblBacteria; AAC22477; AAC22477; HI_0818.
DR   KEGG; hin:HI_0818; -.
DR   PATRIC; fig|71421.8.peg.859; -.
DR   eggNOG; COG2017; Bacteria.
DR   HOGENOM; CLU_031753_1_0_6; -.
DR   OMA; ATWLSCK; -.
DR   PhylomeDB; P31765; -.
DR   BioCyc; HINF71421:G1GJ1-859-MON; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004034; F:aldose 1-epimerase activity; IBA:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IBA:GO_Central.
DR   GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR   Gene3D; 2.70.98.10; -; 1.
DR   InterPro; IPR018052; Ald1_epimerase_CS.
DR   InterPro; IPR013458; Ald_epimerase_bac.
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   TIGRFAMs; TIGR02636; galM_Leloir; 1.
DR   PROSITE; PS00545; ALDOSE_1_EPIMERASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Isomerase; Reference proteome.
FT   CHAIN           1..340
FT                   /note="Aldose 1-epimerase"
FT                   /id="PRO_0000197445"
FT   ACT_SITE        172
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10126"
FT   ACT_SITE        305
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         243
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   VARIANT         42
FT                   /note="V -> I (in strain: RM 7004)"
FT   VARIANT         46
FT                   /note="D -> G (in strain: RM 7004)"
FT   VARIANT         58
FT                   /note="D -> E (in strain: RM 7004)"
FT   VARIANT         113
FT                   /note="N -> K (in strain: RM 7004)"
SQ   SEQUENCE   340 AA;  38102 MW;  4ECAE4FB8C498C7A CRC64;
     MLEQTTFNAP DGAPYQLITL QNENGMRVQF MDWGATWLSC KVPVNDTLRE VLLGCKVDNY
     PTHQSYLGAS VGRYANRIAN AQFELNGELI KLSSNQGKHQ LHGGEGFDKR RWNIQECGEN
     FVCFSLHSVD GDQGFPGNVD VSVTYTLTGD NSVKIEYAGM CDKDTALNLT NHTYFNLENA
     EQGSDVREHT LRLNADFYLP VDNEGIPNSP LKHVVNTSFD FRIAKPIKQD FLQGDQQATK
     GYDHSFIVNK AWQKPCVLLT SPTGDLSLEV RTSQAALQVY TGNYLAGTPT RNGELYADFS
     GIALETQCLP DTPNHPEWQN YGGIQKAGGR YYQWTEFKFK