ID   A0A0U3PJI5_9ACTN        Unreviewed;       543 AA.
AC   A0A0U3PJI5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:ALV33926.1};
GN   ORFNames=AS200_19165 {ECO:0000313|EMBL:ALV33926.1};
OS   Streptomyces sp. CdTB01.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV33926.1, ECO:0000313|Proteomes:UP000068029};
RN   [1] {ECO:0000313|EMBL:ALV33926.1, ECO:0000313|Proteomes:UP000068029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CdTB01 {ECO:0000313|EMBL:ALV33926.1,
RC   ECO:0000313|Proteomes:UP000068029};
RA   Tian Y., Zhou G., Yang H., Lu X.;
RT   "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT   bacterium tolerant to cadmium.";
RL   Submitted (DEC-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}.
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DR   EMBL; CP013743; ALV33926.1; -; Genomic_DNA.
DR   RefSeq; WP_058923582.1; NZ_CP013743.1.
DR   AlphaFoldDB; A0A0U3PJI5; -.
DR   STRING; 1725411.AS200_19165; -.
DR   KEGG; scx:AS200_19165; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000068029; Chromosome.
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; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
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};
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:UP000068029}.
FT   DOMAIN          46..183
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          209..307
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          315..421
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          464..516
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   543 AA;  57915 MW;  4B20FFF7B56CE003 CRC64;
     MHDDLIARAQ TWLAEDPDPD TRAELSKLIE AGDLTELADR FSGTLQFGTA GLRGELGAGP
     NRMNRSVVIR AAAGLAAHLK ATGHTDGLVV IGYDARHKSA DFARDTAAVM TGAGLKAAVL
     PRPLPTPVLA FAIRHLGAVA GVEVTASHNP PRDNGYKVYL GDGSQIVPPA DAQIAAQIQA
     ITSLHDVPRP ETGWQTLDES VLNAYLARTD AVLAPTSPRT ARTVYTAMHG VGRDTLLAAF
     ARAGFPEPAL VAEQADPDPD FPTVAFPNPE EPGAMDLAFA KARETSPDLI IANDPDADRC
     AVAVKQGADW RMLRGDEVGA LLAAHLVARG AQGTFAESIV SSSLLGRIAE KANLPYEETL
     TGFKWIARVD GLRYGYEEAL GYCVDPEGVR DKDGITAALL ITELASTLKE ENRTLLDLLD
     DLAVEHGLHA TDQLSVRVQD LTIIARAMER LRENPPTTLA GLRVTRAEDL TQGTDKLPPT
     DGLRYTLEGA RVIVRPSGTE PKLKCYLEVV VPLKTHKDLP EAHATADEIL AALKQDLSTA
     AGI
//