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Database: UniProt
Entry: A0A3G6IYT4_9CORY
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ID   A0A3G6IYT4_9CORY        Unreviewed;       458 AA.
AC   A0A3G6IYT4;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Phosphomannomutase/phosphoglucomutase {ECO:0000313|EMBL:AZA10862.1};
DE            EC=5.4.2.2 {ECO:0000313|EMBL:AZA10862.1};
GN   Name=algC {ECO:0000313|EMBL:AZA10862.1};
GN   ORFNames=CGERO_02690 {ECO:0000313|EMBL:AZA10862.1};
OS   Corynebacterium gerontici.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=2079234 {ECO:0000313|EMBL:AZA10862.1, ECO:0000313|Proteomes:UP000271587};
RN   [1] {ECO:0000313|EMBL:AZA10862.1, ECO:0000313|Proteomes:UP000271587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W8 {ECO:0000313|EMBL:AZA10862.1,
RC   ECO:0000313|Proteomes:UP000271587};
RA   Kleinhagauer T., Glaeser S.P., Spergser J., Ruckert C., Kaempfer P.,
RA   Busse H.-J.;
RL   Submitted (NOV-2018) 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}.
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DR   EMBL; CP033897; AZA10862.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3G6IYT4; -.
DR   KEGG; cgk:CGERO_02690; -.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000271587; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004614; F:phosphoglucomutase 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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
DR   PANTHER; PTHR43771:SF1; 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.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AZA10862.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271587}.
FT   DOMAIN          11..127
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          158..257
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          263..371
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          376..457
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   458 AA;  49221 MW;  A9A9D3194453A940 CRC64;
     MRSREAVSNV IKAYDVRGVV GEDIDADFIR DVGAAFGRLM RNESAEQVVI GHDMRPSSPE
     LARAFAEGVT SQGVNAVMIG LSSTDQLYFA SGELDCPGAM FTASHNPAEY NGIKLCRSGA
     RPVGQATGLA DIIDMLVEGV PAYEGEAGAI SERATLEAYG QYLRNLVDLS SIRHLKVAVD
     AANGMAGYTV PEVFKGLNLD IEDLYFELDG TFPNHEANPL DPKNLVDLQA FTPEVGADIG
     LAFDGDADRC FVVDELGQPV SPSAICAIVA QRYLERKPGS TIIHNLITSK TVPDIIREHG
     GTPVRTRVGH SFIKAQMAEH GAVFGGEHSA HYYFQEFFNA DSGILAAMHV LAALGGQDKP
     LSELMAEYTR YAASGEINSK LDSAEAQAER AQAVLDAFAD RAESVDELDG FTVELKGTPA
     WFNVRASNTE PLLRLNVEAP TQDEVDALVS EILAIIRA
//
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