ID   M4U0A6_9XANT            Unreviewed;       720 AA.
AC   M4U0A6;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=glucose-6-phosphate 1-epimerase {ECO:0000256|ARBA:ARBA00012083};
DE            EC=5.1.3.15 {ECO:0000256|ARBA:ARBA00012083};
GN   ORFNames=XAC29_21640 {ECO:0000313|EMBL:AGH79709.1};
OS   Xanthomonas axonopodis Xac29-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=1304892 {ECO:0000313|EMBL:AGH79709.1, ECO:0000313|Proteomes:UP000011979};
RN   [1] {ECO:0000313|EMBL:AGH79709.1, ECO:0000313|Proteomes:UP000011979}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xac29-1 {ECO:0000313|EMBL:AGH79709.1,
RC   ECO:0000313|Proteomes:UP000011979};
RA   Chen G., Zou H., Ye G., Song X., Ji Z., Ma W.;
RT   "Completed genome of Xanthomonas axonopodis sp. Xac29-1.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP004399; AGH79709.1; -; Genomic_DNA.
DR   RefSeq; WP_011052877.1; NC_020800.1.
DR   AlphaFoldDB; M4U0A6; -.
DR   GeneID; 66913272; -.
DR   KEGG; xao:XAC29_21640; -.
DR   PATRIC; fig|1304892.4.peg.4523; -.
DR   HOGENOM; CLU_020479_0_0_6; -.
DR   Proteomes; UP000011979; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0047938; F:glucose-6-phosphate 1-epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd09020; D-hex-6-P-epi_like; 1.
DR   CDD; cd13399; Slt35-like; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 1.10.8.350; Bacterial muramidase; 1.
DR   Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 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   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR043426; MltB-like.
DR   InterPro; IPR011970; MltB_2.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
DR   InterPro; IPR031304; SLT_2.
DR   NCBIfam; TIGR02283; MltB_2; 1.
DR   PANTHER; PTHR30163; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE B; 1.
DR   PANTHER; PTHR30163:SF8; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE B; 1.
DR   Pfam; PF01263; Aldose_epim; 1.
DR   Pfam; PF01471; PG_binding_1; 1.
DR   Pfam; PF13406; SLT_2; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   SUPFAM; SSF47090; PGBD-like; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..720
FT                   /note="glucose-6-phosphate 1-epimerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004059061"
FT   DOMAIN          25..320
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF13406"
FT   DOMAIN          341..397
FT                   /note="Peptidoglycan binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF01471"
SQ   SEQUENCE   720 AA;  76991 MW;  44017743DA4AACEF CRC64;
     MTLSRGALPF VLGLLPLAAC ADPAFDRCLA GLQTQAAAKG VDAASFQRFT AGLAPDSSVL
     PLLDAQPEFT TPIWDYLASL VDSQRVTDGQ AMLVTHRELL SRLSDQTGVD PATIVAVWGV
     ESDYGRVTGK RPLLVSLATL SCAGRRQPFF RGEFLALLSL LQQGDLSADG LTGSWAGAFG
     QTQFMPSTYA RIAVDGDGDG RRDLVTSIPD ALASTANYLV KAGWERARPW GMEVTLPRGF
     DASKAGRTRR QPLQAWQSAG LLGTDGKPLA PTGLPAETPA ALLLPAGATG PAFLVFRNYD
     AIYAYNAAES YALSIALLAD RLRGGAGLIA AWPTDDPGLG RPERRELQQL LLARGYQIGE
     ADGMVGSATR RAIQVEQTRL GLQPADGRPG QRILAALRAA PPVAGAAAMR ATAFKLPAAY
     PAFAQSPSVQ KASPMSDTTG LTTGDFHGFP SLLIDTPFST AAISLFGGQL LSFVPEGGQD
     VMWLSPSAQQ PPTPIRGGAP VCWPYFGRQD QAGDVPAHGF VRTVAWQLTE SHREDDGTVV
     LTLTPPRFDD LALRLRMTLR IGRTLEQRLI TENTSVAPVR FTQALHNYFR VGDALKVSVQ
     GLDGLDYLDK YENYATAHRQ QGDWSLRDPR DPGRSDRIYT NAGGRYTLTD PVLGRRIVIA
     TEGSRSLVAW NPGEDAGKKM ADVGEGWRDY VCLEAANAGP DVIELAPGAS HTLTQTISVE
//