ID A0A0U1Q0T4_9BURK Unreviewed; 461 AA.
AC A0A0U1Q0T4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KKW68378.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:KKW68378.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:KKW68378.1};
GN ORFNames=AAV94_05845 {ECO:0000313|EMBL:KKW68378.1};
OS Lampropedia cohaerens.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Lampropedia.
OX NCBI_TaxID=1610491 {ECO:0000313|EMBL:KKW68378.1, ECO:0000313|Proteomes:UP000050580};
RN [1] {ECO:0000313|EMBL:KKW68378.1, ECO:0000313|Proteomes:UP000050580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT6 {ECO:0000313|EMBL:KKW68378.1,
RC ECO:0000313|Proteomes:UP000050580};
RA Tripathi C., Rani P., Mahato N.K., Lal R.;
RT "Draft genome sequence of Lampropedia sp. CT6, isolated from the microbial
RT mat of a hot water spring, located at Manikaran, India.";
RL Submitted (MAY-2015) 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:KKW68378.1}.
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DR EMBL; LBNQ01000020; KKW68378.1; -; Genomic_DNA.
DR RefSeq; WP_046741440.1; NZ_LBNQ01000020.1.
DR AlphaFoldDB; A0A0U1Q0T4; -.
DR STRING; 1610491.AAV94_05845; -.
DR PATRIC; fig|1610491.3.peg.1242; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000050580; 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:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
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; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR43771:SF2; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 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, ECO:0000313|EMBL:KKW68378.1};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000050580}.
FT DOMAIN 7..134
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 153..250
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 255..361
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 369..448
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 461 AA; 49688 MW; 1D071BDDB77CB2DC CRC64;
MQVSASIFKA YDIRGIVPTT LTPDIARALG RAFGTVALQQ GEREVAVGRD GRLSGPQLSA
ALIAGLTDVG VDVLDIGMVT TPMLYFAAAT HTRSGIQITG SHNPRDYNGF KMVLAGKAIY
GEEIQQLRTL IETDGWQQAS APGRVRQLDV FPQYLQRIAS DIRLARPIKV IVDAGNGVAG
ASAPQVLRAI GCEVTELFTD VDGNFPNHHP DPSKPENLQD LIAALRDSDA ELGLAFDGDG
DRLGIVTKDG KNIFPDRQIM LFARDVLSRV PGGEIIYDVK CTQQLAPAIE AAGGKPVMYK
TGHSLIKARM RETDAPLGGE MSGHIFFKER WYGFDDGTYA ACRLLEILSR SADVSVVLND
LPSSHSTPEM NIACAEGEPH ALVAQLVERA RFDAPAKVCT IDGLRVDWPD GFGLVRASNT
TPVLVLRFEG QTPEALQRIQ AQFLALVRSV KPDAQVAAAA H
//
