ID A0A086D1V7_9GAMM Unreviewed; 554 AA.
AC A0A086D1V7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KFF48421.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:KFF48421.1};
GN ORFNames=GY26_14480 {ECO:0000313|EMBL:KFF48421.1};
OS Gammaproteobacteria bacterium MFB021.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1492922 {ECO:0000313|EMBL:KFF48421.1, ECO:0000313|Proteomes:UP000028732};
RN [1] {ECO:0000313|EMBL:KFF48421.1, ECO:0000313|Proteomes:UP000028732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MFB021 {ECO:0000313|EMBL:KFF48421.1,
RC ECO:0000313|Proteomes:UP000028732};
RA Joseph T.C., Baby A., Varghese A.M., Reghunathan D., Murugadas V.,
RA Lalitha K.V.;
RT "Draft Genome sequence of a halophilic and highly halotolerant unknown
RT Gammaproteobacteria strain MFB021.";
RL Submitted (JUN-2014) 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:KFF48421.1}.
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DR EMBL; JNVT01000096; KFF48421.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A086D1V7; -.
DR STRING; 1492922.GY26_14480; -.
DR eggNOG; COG0033; Bacteria.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000028732; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05801; PGM_like3; 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; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005852; PGM_a-D-Glc-sp.
DR NCBIfam; TIGR01132; pgm; 1.
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 Pfam; PF00408; PGM_PMM_IV; 1.
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, ECO:0000313|EMBL:KFF48421.1};
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}.
FT DOMAIN 41..187
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 218..321
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 329..449
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 492..547
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 554 AA; 59779 MW; C0460D297F301303 CRC64;
MSIDPQAGRL PDPHSLANLP RLVSRYYSER PDAHDPAQQV AFGTSGHRGS SLKLSFNEWH
ILATTQAICE YREAQGIDGP LFIGMDTHAL SEPAFVSALE VLAANRVAVR IDAGCEATGF
EPGYTPTPAI SNAILSYNQG RHHGLADGIV ITPSHNPPVD GGFKYNPTNG GPADTGVTQW
IQARANEHLA EGLRQVQRVS YAEALAASTT QRFDYIESYV GGLDKVIDMA AIRDSGFTFG
VDPLGGAGVH YWPRIAEKYD LPLEVLSTTV DPTFRFMRVD WDGKIRMDCS SPHAMAGLIE
NKDRFDVSFA CDTDHDRHGI VARSTGLLNP NHYLAVAIEY LFTHRPHWGD QAAIGKTLVS
SSMIDRVAEG LGREVTEVPV GFKWFVDGLI EGSLGFGGEE SAGASFLTLE GQPWSTDKDG
IILGLLAAEI TAVTGQDPGE RYRALTERYG APVYQRVDAP ATREQKAKLG KLSPEQVTAE
TLAGHPIMRK LTEAPGNGAA IGGLKVVTEA GWFAARPSGT EDVYKIYAES FEGEAHLARI
QQEAKALVDA VLAG
//
