ID A0A1I5AG69_9FLAO Unreviewed; 576 AA.
AC A0A1I5AG69;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:SFN61418.1};
GN ORFNames=SAMN05421741_10835 {ECO:0000313|EMBL:SFN61418.1};
OS Paenimyroides ummariense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Paenimyroides.
OX NCBI_TaxID=913024 {ECO:0000313|EMBL:SFN61418.1, ECO:0000313|Proteomes:UP000199036};
RN [1] {ECO:0000313|Proteomes:UP000199036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-12 {ECO:0000313|Proteomes:UP000199036};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FOVI01000008; SFN61418.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5AG69; -.
DR STRING; 913024.SAMN05421741_10835; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000199036; Unassembled WGS sequence.
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}.
FT DOMAIN 47..184
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 224..316
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 322..441
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 576 AA; 64107 MW; 7741EBED1FA7F424 CRC64;
MEIPKNILEH SNKWIQDPFD VETQNLVKEL LTSSPKELED AFYRNLEFGT GGMRGIMGVG
TNRINKYTLG KNTQGLSQYL KQSFPNEQIK VAIAYDCRHN SKSLAKVVAD VFSANGIKVF
LFEDLRPTPE LSFAVRYLNC HAGIVLTASH NPPEYNGYKV YWQDGGQLVP PQDKEIIQVI
DSLDYSDILF DSNPELIEYI GAEIDEAFAQ SSIENATFNL PEGARENLKI VYTSLHGTSI
KAIPNVLEKA GYTNVNIVAE QAEPNGDFPT VKSPNPEEPE ALKMAIDLAN ETNADIVIGT
DPDSDRLGIA VRDNEGKMIL LNGNQAMVVM TAFLLEQWKR DGKFEGKKHF IGSTIVSTPM
ILALAEAYEV DCKVGLTGFK WIAKFIKDFP EQKFIGGGEE SFGYMVGDAV RDKDAVASTL
LICEIAAIAK ASGSSVYKEL QNLYADFGYY KEHLISLTKK GKDGAEEIAT MMTELRNNPL
KEIAGERVVF VEDYQSSIAT NLFSNETEPL FLPKSNVLIY YLEDGSKICA RPSGTEPKIK
FYFSTNTPIE NVEEIKDADE YLTDKIQSII NDMNLN
//
