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Database: UniProt
Entry: E1SMT0_FERBD
LinkDB: E1SMT0_FERBD
Original site: E1SMT0_FERBD 
ID   E1SMT0_FERBD            Unreviewed;       266 AA.
AC   E1SMT0;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Putative glucose-6-phosphate 1-epimerase {ECO:0000256|PIRNR:PIRNR016020};
DE            EC=5.1.3.15 {ECO:0000256|PIRNR:PIRNR016020};
GN   OrderedLocusNames=Fbal_2397 {ECO:0000313|EMBL:ADN76599.1};
OS   Ferrimonas balearica (strain DSM 9799 / CCM 4581 / KCTC 23876 / PAT).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Ferrimonadaceae; Ferrimonas.
OX   NCBI_TaxID=550540 {ECO:0000313|EMBL:ADN76599.1, ECO:0000313|Proteomes:UP000006683};
RN   [1] {ECO:0000313|EMBL:ADN76599.1, ECO:0000313|Proteomes:UP000006683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9799 / CCM 4581 / KCTC 23876 / PAT
RC   {ECO:0000313|Proteomes:UP000006683};
RX   DOI=10.4056/sigs.1161239;
RA   Nolan M., Sikorski J., Davenport K., Lucas S., Glavina Del Rio T., Tice H.,
RA   Cheng J., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y., Jeffries C., Tapia R., Brettin T., Detter J., Han C.,
RA   Yasawong M., Rohde M., Tindall B., Goker M., Woyke T., Bristow J.,
RA   Eisen J., Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Lapidus A.;
RT   "Complete genome sequence of Ferrimonas balearica type strain (PAT).";
RL   Stand. Genomic Sci. 3:174-182(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 6-phosphate = beta-D-glucose 6-phosphate;
CC         Xref=Rhea:RHEA:16249, ChEBI:CHEBI:58225, ChEBI:CHEBI:58247;
CC         EC=5.1.3.15; Evidence={ECO:0000256|ARBA:ARBA00001096};
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate 1-epimerase family.
CC       {ECO:0000256|ARBA:ARBA00005866, ECO:0000256|PIRNR:PIRNR016020}.
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DR   EMBL; CP002209; ADN76599.1; -; Genomic_DNA.
DR   RefSeq; WP_013345905.1; NC_014541.1.
DR   AlphaFoldDB; E1SMT0; -.
DR   STRING; 550540.Fbal_2397; -.
DR   GeneID; 67184043; -.
DR   KEGG; fbl:Fbal_2397; -.
DR   eggNOG; COG0676; Bacteria.
DR   HOGENOM; CLU_048345_3_0_6; -.
DR   OMA; TQALHSY; -.
DR   Proteomes; UP000006683; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0047938; F:glucose-6-phosphate 1-epimerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd09020; D-hex-6-P-epi_like; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   InterPro; IPR008183; Aldose_1/G6P_1-epimerase.
DR   InterPro; IPR025532; G6P_1-epimerase.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   PANTHER; PTHR11122; APOSPORY-ASSOCIATED PROTEIN C-RELATED; 1.
DR   PANTHER; PTHR11122:SF39; GLUCOSE-6-PHOSPHATE 1-EPIMERASE; 1.
DR   Pfam; PF01263; Aldose_epim; 1.
DR   PIRSF; PIRSF016020; PHexose_mutarotase; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|PIRNR:PIRNR016020};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006683}.
FT   ACT_SITE        141
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
FT   ACT_SITE        240
FT                   /evidence="ECO:0000256|PIRSR:PIRSR016020-1"
SQ   SEQUENCE   266 AA;  28588 MW;  18F6460DF3ADBD5E CRC64;
     MSPLILHCAD SQLTVSPFGA QALSWQVAGQ ERLWLSLDAD LDGHHPIRGG VPLCFPWFGK
     AAQGPSHGFA RTRLWQVAEQ SQTDDHAHLV LSLEQDADTE ALWPHPFRAE MAFTLKANAL
     QLALTVTNPG SAPLSYTAAL HSYLCTDVAQ LRITELAGLP YHDKLSNADC LFEDGPDAAL
     PPIPVDAIVP GLSNCRLAQG NDILKIDNQG HDAAVIWNPG PDHGIGDVHF GGEQAFICIE
     SAHALTPITL APCQRHTLSQ TLTVNA
//
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