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Database: UniProt
Entry: A0A397LCN4_9FLAO
LinkDB: A0A397LCN4_9FLAO
Original site: A0A397LCN4_9FLAO 
ID   A0A397LCN4_9FLAO        Unreviewed;       462 AA.
AC   A0A397LCN4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:RIA09489.1};
GN   ORFNames=OE09_1327 {ECO:0000313|EMBL:RIA09489.1};
OS   Flavobacteriaceae bacterium MAR_2010_72.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1250029 {ECO:0000313|EMBL:RIA09489.1, ECO:0000313|Proteomes:UP000265779};
RN   [1] {ECO:0000313|EMBL:RIA09489.1, ECO:0000313|Proteomes:UP000265779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mar_2010_72 {ECO:0000313|EMBL:RIA09489.1,
RC   ECO:0000313|Proteomes:UP000265779};
RA   Teeling H.;
RT   "A large-scale integrated study on North Sea by COGITO (Coastal Microbe
RT   Genomic & Taxonomic Observatory).";
RL   Submitted (AUG-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RIA09489.1}.
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DR   EMBL; QXCW01000002; RIA09489.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397LCN4; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000265779; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   InterPro; IPR024086; GlmM_arc-type.
DR   NCBIfam; TIGR03990; Arch_GlmM; 1.
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   Pfam; PF00408; PGM_PMM_IV; 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   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004326};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265779}.
FT   DOMAIN          8..140
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          173..263
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          270..375
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          398..456
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   462 AA;  50366 MW;  5C40D587ECF9673B CRC64;
     MTLIKSISGI RGTIGGKMGD NLTPIDAVTF AAAYGTWVKK QRQKEHYRVV VGRDARISGE
     MIQSLVMQTL VGLGIHVIDL GLSTTPTVEV AVPMEHADGG IILTASHNPK QWNALKLLNA
     KGEFLNAEEG ATILAIAEQG EIDFAEVDDL GKITKNQAYI DLHIDEVLNL DLVNVKAIEK
     AKFKVVVDGV NSTGGIAIPL LLERLGVHPV KLYCEPNGHF PHNPEPLKEH LTDLSKAVVS
     EHADFGIVVD PDVDRLAFID EKGEMFGEEY TLVACADYVL SKTPGNTVSN MSSTRALSDV
     TKQHGGNYEA SAVGEVNVVE LMKKNNAVIG GEGNGGIIYP ELHYGRDALV GVALFLSLLA
     EKKMNVSDLR ASYPNYFMSK KKIELTPSLN VDGILKSMED RYSHEKLTTI DGVKIDFSKS
     WVHLRKSNTE PIIRIYTEAP SQVEADTLAD RIISEIKSIA NI
//
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