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Database: UniProt
Entry: A0A1E3VPL9_9HYPH
LinkDB: A0A1E3VPL9_9HYPH
Original site: A0A1E3VPL9_9HYPH 
ID   A0A1E3VPL9_9HYPH        Unreviewed;       500 AA.
AC   A0A1E3VPL9;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   02-APR-2025, entry version 24.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:ODR95462.1};
GN   ORFNames=AUC71_04830 {ECO:0000313|EMBL:ODR95462.1};
OS   Methyloceanibacter marginalis.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Hyphomicrobiaceae; Methyloceanibacter.
OX   NCBI_TaxID=1774971 {ECO:0000313|EMBL:ODR95462.1, ECO:0000313|Proteomes:UP000095042};
RN   [1] {ECO:0000313|EMBL:ODR95462.1, ECO:0000313|Proteomes:UP000095042}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R-67177 {ECO:0000313|EMBL:ODR95462.1,
RC   ECO:0000313|Proteomes:UP000095042};
RX   PubMed=27501305; DOI=10.1111/1462-2920.13485;
RA   Vekeman B., Kerckhof F.M., Cremers G., de Vos P., Vandamme P., Boon N.,
RA   Op den Camp H.J., Heylen K.;
RT   "New Methyloceanibacter diversity from North Sea sediments includes
RT   methanotroph containing solely the soluble methane monooxygenase.";
RL   Environ. Microbiol. 18:4523-4536(2016).
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}.
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:ODR95462.1}.
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DR   EMBL; LPWD01000464; ODR95462.1; -; Genomic_DNA.
DR   RefSeq; WP_069625154.1; NZ_LPWD01000464.1.
DR   AlphaFoldDB; A0A1E3VPL9; -.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000095042; Unassembled WGS sequence.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
DR   PANTHER; PTHR43771:SF2; PHOSPHOMANNOMUTASE_PHOSPHOGLUCOMUTASE; 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.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095042}.
FT   DOMAIN          27..158
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          177..273
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          279..390
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          415..485
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   500 AA;  54839 MW;  7F8C6837ADF8B6D6 CRC64;
     MFPKPRQDLV PNTAEFERLP LVKVTGFREY DARWLYPQEV NLLGMEAVGL GLTTLMRERG
     VPVRIVVGHD FRSYSAAIKA ALVTGLLAGG ARCHDIGLAL SPMAYFAQFD LDVEGVAMVT
     ASHNDNGWTG IKMGIDRPLT FSPEDMTALK EIVMNAKFAP YHEGARYIYV PDMPERYMAD
     LLKHPKLTRR LKVVVSCGNG TAGAFAPHVL SALGCEVIPL NCELDHSFPA HNPNPEDLAM
     LNATRDAVME HKADLALVFD GDGDRCGVVD NTGEAIYADK VGVMLARDIS ALNKNAHFVV
     DVKSTGLFKT DPVLQANGAK TDYWKTGHSY IKRYSHETGA LVGFEKSGHF FFNPPIGRGY
     DDGLVAATAV LDMLDRNPDK TLAELKDALP RTWQSPTMSP HCADEAKYGV VDRVVKHFED
     VAANGGKLAG QNIRELITVN GIRIVLDDGT WGLVRASSNK PELVVVVESP TSEENMRAIF
     AEIDKELSKQ PEVGEYNQKI
//
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