ID A3TG97_9MICO Unreviewed; 554 AA.
AC A3TG97;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:EAP99857.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:EAP99857.1};
GN ORFNames=JNB_06799 {ECO:0000313|EMBL:EAP99857.1};
OS Janibacter sp. HTCC2649.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=313589 {ECO:0000313|EMBL:EAP99857.1, ECO:0000313|Proteomes:UP000005063};
RN [1] {ECO:0000313|EMBL:EAP99857.1, ECO:0000313|Proteomes:UP000005063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2649 {ECO:0000313|EMBL:EAP99857.1,
RC ECO:0000313|Proteomes:UP000005063};
RX PubMed=21075932; DOI=10.1128/JB.01298-10;
RA Thrash J.C., Cho J.C., Bertagnolli A.D., Ferriera S., Johnson J.,
RA Vergin K.L., Giovannoni S.J.;
RT "Genome sequence of the Marine Janibacter Sp. Strain HTCC2649.";
RL J. Bacteriol. 193:584-585(2011).
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:EAP99857.1}.
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DR EMBL; AAMN01000001; EAP99857.1; -; Genomic_DNA.
DR RefSeq; WP_009775664.1; NZ_CH672413.1.
DR AlphaFoldDB; A3TG97; -.
DR STRING; 313589.JNB_06799; -.
DR eggNOG; COG0033; Bacteria.
DR HOGENOM; CLU_016950_8_1_11; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000005063; 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:EAP99857.1};
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:UP000005063}.
FT DOMAIN 40..188
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 217..322
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 328..447
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 491..548
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 554 AA; 58545 MW; 31CE5DDDA2E3C8EF CRC64;
MTESRAGQLA QPSDLVDLPH LVTAYYELKP DPDNIDQQVA FGTSGHRGSS LNTAFNEDHI
LATTQAIVDY RKSQGFDGPL FLGRDTHGLS EPAWASALEV LVANDVTVLV DSADRYTPTP
AVSHAILTAN RGKVTGVDGV PAGAGLADGI VVTPSHNPPY DGGFKYNPPH GGPADSDATK
IIAARANELI RAGLEGVKRI PFSRARAGAQ SYDFMGTYVD DLPNVVDLAR IKDAGIRIGA
DPLGGAAVDY WGAIADRHGI DLTVVNPLVD ATWRFMTLDW DEKIRMDCSS PSAMASLIKR
KDEYDIATGN DADSDRHGIV TPDAGLMNPN HYLAVAIQYL YGGARPQWRE DGYIGKTLVS
SSMIDRVAAD LGRRLVEVPV GFKWFVPGLL DGSGPFGGEE SAGASFLRMD GSVWTTDKDG
IILALLASEI LAATGKSPSQ HYGELTAKHG TPAYARIDAP ANREQKAKLG ALTPDAVTAE
SLAGEPITAK LTEAPGNGAA IGGLKVVTES AWFAARPSGT EDVYKIYAES FKGAEHLAQV
QAEAKDVVSA ALGA
//
