ID A0A2R5F3C6_9PROT Unreviewed; 543 AA.
AC A0A2R5F3C6;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000256|ARBA:ARBA00012728};
DE EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
GN Name=pgm {ECO:0000313|EMBL:GBG12629.1};
GN ORFNames=NMK_0160 {ECO:0000313|EMBL:GBG12629.1};
OS Novimethylophilus kurashikiensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Novimethylophilus.
OX NCBI_TaxID=1825523 {ECO:0000313|EMBL:GBG12629.1, ECO:0000313|Proteomes:UP000245081};
RN [1] {ECO:0000313|EMBL:GBG12629.1, ECO:0000313|Proteomes:UP000245081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=La2-4 {ECO:0000313|EMBL:GBG12629.1,
RC ECO:0000313|Proteomes:UP000245081};
RX PubMed=29411502; DOI=10.1111/1462-2920.14062;
RA Lv H., Sahin N., Tani A.;
RT "Isolation and genomic characterization of Novimethylophilus kurashikiensis
RT gen. nov. sp. nov., a new lanthanide-dependent methylotrophic species of
RT Methylophilaceae.";
RL Environ. Microbiol. 20:1204-1223(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC EC=5.4.2.2; Evidence={ECO:0000256|ARBA:ARBA00000443};
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:GBG12629.1}.
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DR EMBL; BDOQ01000001; GBG12629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R5F3C6; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000245081; 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; cd03085; PGM1; 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 InterPro; IPR045244; PGM.
DR PANTHER; PTHR22573:SF2; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 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 Isomerase {ECO:0000313|EMBL:GBG12629.1};
KW Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000245081}.
FT DOMAIN 14..153
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 184..286
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 295..407
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 543 AA; 58558 MW; 7F53889DE0A51CEC CRC64;
MTVRTIATTP FSDQKPGTSG LRKKVPVFQQ PHYLENFVQS IFNSIGAPTG STLVLGGDGR
YYNREAIQII LKMAASNGFG RVLVGKGGIL STPAASCVIR KYKTFGGIIL SASHNPGGPE
GDFGIKYNVT NGGPAPEKVT EEIFARSKTI DEYRILEAAD VALDQLGESR LGDMIVQVID
PVADYAELME SLFDFGAIRS LLAGGFRLRF DAMHAVTGPY AREIIEKRLG AATGSVMNAE
PLPDFGNGHP DPNLTYAHEL VEIVYGDNAP DFGAASDGDG DRNMILGKRF FVTPSDSLAL
LAANATLVPG YKNGLAGIAR SMPTSAAADR VAQALGIPCF ETPTGWKFFG NLMDAGKVTL
CGEESFGTGS DHVREKDGLW AVLFWLNILA VRKQPVEAIM HEHWAKFGRN VYSRHDYEGL
PTDAANGLMQ HLHESFAELV GKQFGDYKVL FCDDFSYTDP VDGSVSTGQG VRIGFVDGSR
IVFRLSGTGT EGATLRIYLE AFEPDISRHH LDAQQALASL IAIASEVSQL KARTGRDHPT
VIT
//
