ID U5S9W5_9LACT Unreviewed; 508 AA.
AC U5S9W5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:AGY81851.1};
GN ORFNames=Q783_06195 {ECO:0000313|EMBL:AGY81851.1};
OS Carnobacterium inhibens subsp. gilichinskyi.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1266845 {ECO:0000313|EMBL:AGY81851.1, ECO:0000313|Proteomes:UP000017469};
RN [1] {ECO:0000313|EMBL:AGY81851.1, ECO:0000313|Proteomes:UP000017469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WN1359 {ECO:0000313|EMBL:AGY81851.1,
RC ECO:0000313|Proteomes:UP000017469};
RX PubMed=24285647;
RA Leonard M.T., Panayotova N., Farmerie W.G., Triplett E.W., Nicholson W.L.;
RT "Complete Genome Sequence of Carnobacterium gilichinskyi Strain WN1359T
RT (DSM 27470T).";
RL Genome Announc. 1:e00985-13(2013).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231}.
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DR EMBL; CP006812; AGY81851.1; -; Genomic_DNA.
DR AlphaFoldDB; U5S9W5; -.
DR STRING; 1266845.Q783_06195; -.
DR KEGG; caw:Q783_06195; -.
DR PATRIC; fig|1266845.5.peg.1165; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_6_0_9; -.
DR Proteomes; UP000017469; Chromosome.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03089; PMM_PGM; 1.
DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
PE 3: Inferred from homology;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 11..150
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 174..282
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 288..399
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 508 AA; 56022 MW; D4B741ABBA7C96B3 CRC64;
MPEFDLASLQ NGSDIRGIAL ETPEHEVTLT DERVEKIAYG FAVWLKEVKK IVVEDEHAPA
KVSVGHDSRL SADRIKSIFI KGLTKAGIDV IDVGLSTTPA MFMSTQYEAY KCDGAVMITA
SHLPFEYNGL KFFTKDGGAE HEDIDFILQQ ADEENITWKN KEGNVTKASL LNEYAKDLVN
KIRLGINDAK QYDQPLTGRH IVVDAGNGAG GFFAEEVLVP LGADISGSQY LNPDGHFPNH
IPNPDNKEAM KSIQDAVIKY HADMGVIFDT DVDRSALVDS NGDTLNRNNL IAVISAILIK
ENPGTTIVTS SATSEHLKTF ITSLGGKQDR YITGYRNVIN RGIQLNKEGT PTSLAIETSG
HAALSENYFL DDGAYLVAKI LMADAGLKKE RKNFSDLITS LKQPVETDEV RFKILSKDVQ
ATGQRVMENF QAYIETATDL TVEPANLEGV RVNTSGQYGI GWMLLRMSLH EPLLVLNLES
DQEGSIKLVR EKLKTFFYDQ SVLDSSRL
//
