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Database: UniProt
Entry: F0J5F6_ACIMA
LinkDB: F0J5F6_ACIMA
Original site: F0J5F6_ACIMA 
ID   F0J5F6_ACIMA            Unreviewed;       341 AA.
AC   F0J5F6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Aldose 1-epimerase {ECO:0000256|ARBA:ARBA00014165, ECO:0000256|PIRNR:PIRNR005096};
DE            EC=5.1.3.3 {ECO:0000256|ARBA:ARBA00013185, ECO:0000256|PIRNR:PIRNR005096};
GN   Name=mro {ECO:0000313|EMBL:BAJ80205.1};
GN   OrderedLocusNames=ACMV_08580 {ECO:0000313|EMBL:BAJ80205.1};
GN   ORFNames=Apmu_0040_03 {ECO:0000313|EMBL:GAN72951.1};
OS   Acidiphilium multivorum (strain DSM 11245 / JCM 8867 / NBRC 100883 / AIU
OS   301).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidiphilium.
OX   NCBI_TaxID=926570 {ECO:0000313|EMBL:BAJ80205.1, ECO:0000313|Proteomes:UP000007100};
RN   [1] {ECO:0000313|EMBL:BAJ80205.1, ECO:0000313|Proteomes:UP000007100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AIU301 {ECO:0000313|EMBL:BAJ80205.1}, and DSM 11245 / JCM 8867
RC   / AIU301 {ECO:0000313|Proteomes:UP000007100};
RA   Narita-Yamada S., Nakamura S., Ito N., Takarada H., Katano Y., Nakazawa H.,
RA   Hosoyama A., Yamada R., Fujita N.;
RT   "Whole genome sequence of Acidiphilium multivorum AIU301.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAN72951.1, ECO:0000313|Proteomes:UP000032662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AIU301 {ECO:0000313|EMBL:GAN72951.1,
RC   ECO:0000313|Proteomes:UP000032662};
RA   Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT   "Whole genome sequence of Acidiphilium multivorum AIU301.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00001614,
CC         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; AP012035; BAJ80205.1; -; Genomic_DNA.
DR   EMBL; BANA01000040; GAN72951.1; -; Genomic_DNA.
DR   RefSeq; WP_013639661.1; NZ_BANA01000040.1.
DR   AlphaFoldDB; F0J5F6; -.
DR   KEGG; amv:ACMV_08580; -.
DR   HOGENOM; CLU_031753_2_0_5; -.
DR   OrthoDB; 9779408at2; -.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000007100; Chromosome.
DR   Proteomes; UP000032662; Unassembled WGS sequence.
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; 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; 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.
DR   PROSITE; PS00545; ALDOSE_1_EPIMERASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR005096};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PIRNR:PIRNR005096}.
FT   ACT_SITE        184
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   ACT_SITE        302
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-1"
FT   BINDING         81..82
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         184..186
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-3"
FT   BINDING         244
FT                   /ligand="beta-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:27667"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005096-2"
SQ   SEQUENCE   341 AA;  35939 MW;  549C369534B1030B CRC64;
     MPEPVIAPYG TTRAGAKVRR ITLANAAGMS VSLLDYGGIV DELLAPDRRG RLANVVLSCP
     TLADYETKSP YFGALVGRYA NRIAGAAFTL DGVRHTLPAN EGANTLHGGP ADGPAPNFSH
     RVWDIVAATG SALTLRLHSP DGENGFPGDL TVYVTYTLTP DNTLRLDYAA RVAGRATVLN
     LTNHAYFNLA GGGTALDHEI AVAAARYLAP DAANIPTGAI APVAGTWLDL TRQQRIGPAR
     AGLDHCFVLD KPEGVIGPAA LLRDPASGRV LAVETTEPAV QVYAAGKLDL PPYGPGDGIA
     LETQHFPDSP NRPAFPSTRL DPGEAFRSST VWRFTTDQTR T
//
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