ID A4TEX9_MYCGI Unreviewed; 529 AA.
AC A4TEX9;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain I {ECO:0000313|EMBL:ABP47299.1};
GN OrderedLocusNames=Mflv_4831 {ECO:0000313|EMBL:ABP47299.1};
OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS PYR-GCK)).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP47299.1};
RN [1] {ECO:0000313|EMBL:ABP47299.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP47299.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABP47299.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP47299.1};
RX PubMed=23469141;
RA Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.;
RT "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage
RT Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH
RT during Pyrene Degradation.";
RL PLoS ONE 8:E58066-E58066(2013).
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}.
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DR EMBL; CP000656; ABP47299.1; -; Genomic_DNA.
DR AlphaFoldDB; A4TEX9; -.
DR STRING; 350054.Mflv_4831; -.
DR KEGG; mgi:Mflv_4831; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_0_2_11; -.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05799; PGM2; 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 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 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 Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326}.
FT DOMAIN 38..172
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 201..290
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 303..417
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 529 AA; 55307 MW; 1600B0493374C403 CRC64;
MHTAVEEWLA HDPDPESAAE LAACDDDELA ERFAHTLTFG TAGLRGPLRA GPNGMNLAVV
IRATWAVARV LTDRSPASSQ VVVGYDARHR SAEFGRAAAE VFAAQGFTVQ LMSGPVPTPA
VAFAVRHLGA AAGVQITASH NPPTDNGYKV YVTGGLQIVS PTDREIEAAI AAAPPADEIP
RAPVEVPAAD ELRAYLERAA SVRHAAGAAR IALTPMHGVG GEFALDALAL AGFADVHVVE
EQFAPDPDFP TVAFPNPEEP GASDALLALA AGVDAEIAIA LDPDADRCAI GVPTPTGWRM
LSGDETGWLL GDYVLSHADP THAVVASTVV SSRMLASIAA AHGARHVETL TGFKWLARAD
EGLDATLVYA YEEAIGHCVD PGAVRDKDGI SAAVLACDLV VSLREQGRTL LDALDDLARR
HGVHTTTAVT RRVRSPQDAA AMMSRLRAAP PEEIAGFAVT VTDLMPRTDA LIFSGGDSAT
SVRVVMRPSG TEPKLKSYIE IRCTGEVATG RSHAADVQDA VAAAIATWR
//
