ID A0A249T4X7_9BACT Unreviewed; 573 AA.
AC A0A249T4X7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:ASZ14946.1};
GN ORFNames=CK934_14350 {ECO:0000313|EMBL:ASZ14946.1};
OS Chitinophaga sp. MD30.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=2033437 {ECO:0000313|EMBL:ASZ14946.1, ECO:0000313|Proteomes:UP000217148};
RN [1] {ECO:0000313|EMBL:ASZ14946.1, ECO:0000313|Proteomes:UP000217148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD30 {ECO:0000313|EMBL:ASZ14946.1,
RC ECO:0000313|Proteomes:UP000217148};
RA Wan X., Darris M., Hou S., Donachie S.P.;
RT "Draft genome sequence of a novel Chitinophaga sp., MD30, isolated from a
RT biofilm in an air conditioner condensate pipe.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|RuleBase:RU004326}.
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DR EMBL; CP023254; ASZ14946.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A249T4X7; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000217148; Chromosome.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05799; PGM2; 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; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 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.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Reference proteome {ECO:0000313|Proteomes:UP000217148}.
FT DOMAIN 44..181
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 206..307
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 319..443
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 573 AA; 63298 MW; 449D00FD8F00CD0D CRC64;
MDINIESKVA QWLSGQFDAD TVAAVKDLQQ RPEELADAFY RNLEFGTGGL RGIMGVGTNR
MNKYTVGMAT QGFANYLRQA FDGEVKIAIA HDSRNNSRYF AEVAANVMAA NGIKVLLFES
LRPTPELSFT IRHHQCQGGI VLTASHNPRE YNGYKAYWND GAQLIPPHDK NVIREVEQIS
SVDEVKWSGG EANITSIGKA EDEAYLQVLK GLSIHPDVIA SQHDLKIVYT PIHGTGITLV
PEILQRFGFT NVHVVEEQAT PDGNFPTVVY PNPEEAEAMS MGLKKAKELD AAILLGTDPD
ADRVGIAVKD LQGEWILLNG NQTAVLLFNY IIEGRKQKGL AQPNDYVCKT VVTSDLIDVF
AAKNGVACYN VLTGFKWIAE LIREKEGKEQ FICGGEESYG YMIGDRVRDK DAVASVAMIC
EMAAFARSQG RSLYEQLIDI YVKYGFYKEH LISITRKGMK GAEEIAEMMR GYRENPPTEI
NGAAVVAVYD YQLQQIKDLK SGETKAIALP KSNVLQFVLA DGSKISARPS GTEPKIKFYF
SVHQPLDSAA HFDIVNGQLD QRIQGIISGL KLN
//
