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Database: UniProt
Entry: A0A1G6ZKT4_9ACTO
LinkDB: A0A1G6ZKT4_9ACTO
Original site: A0A1G6ZKT4_9ACTO 
ID   A0A1G6ZKT4_9ACTO        Unreviewed;       692 AA.
AC   A0A1G6ZKT4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:SDE03120.1};
GN   ORFNames=SAMN05421878_101158 {ECO:0000313|EMBL:SDE03120.1};
OS   Actinobaculum suis.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinobaculum.
OX   NCBI_TaxID=1657 {ECO:0000313|EMBL:SDE03120.1, ECO:0000313|Proteomes:UP000182744};
RN   [1] {ECO:0000313|Proteomes:UP000182744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20639 {ECO:0000313|Proteomes:UP000182744};
RA   Varghese N.;
RL   Submitted (OCT-2016) 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; FNAU01000001; SDE03120.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6ZKT4; -.
DR   Proteomes; UP000182744; Unassembled WGS sequence.
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; 4.
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};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182744}.
FT   DOMAIN          99..214
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          327..413
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          483..574
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          639..660
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          281..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   692 AA;  71631 MW;  79DEF3E1335871DD CRC64;
     MSEETSAGAA TEAMREDAAT ETTPVTPDSA DVTPDSADVM PDGADITPDL AEVIARAREW
     ALHDPDPVTR AELEAVLARA ETDAAAAQEL REAFAGPLHF GTAGLRGRMG FGESRMNRAV
     VIRATAGLMA WLKERVREPI VVVGCDARHG SADFARAAVQ VISAAGGRAL ALPERLPTPV
     TAYAVKKLGA DAGVMVTASH NPAQDNGYKV YLGGRVAGGP GAGVQIVPPV DTEIADLIAA
     APPADEVAQD RERVSAVDVV ADYVAETAEL VRAMVSAGTA SPGTAGASCA DSGSADVSAA
     GSGADGPHVA GAQTTNAAEN STGADVPGAD LRIVLTPMHG VGARVALEVL RASGFAHVHV
     VPEQVEPDPD FPTVAFPNPE EQGALDLAIA LAREESADIV LALDPDADRC SAAVPWGSAG
     QWRQLSGDEI GALLGNWIAS KTTPAAPAQT AELVEQVAGP GKQMAGPGTA LRAQTAELVS
     SRRVLANSIV SSRLLAEIAR KHGLDYAVTL TGFKWIARVP DLLFGYEEAI GFCVNPGAVA
     DKDGVSACAL LARIAADLKA QGSSVQAYLD EIAREYGLYA TAPLTFRVAD LSLISKGMQQ
     LRANPPRQLV GSPVTVFADL AEGYGEVPPT DGILMLTEAN DRVVVRPSGT EPKLKCYLEV
     VFAPSQEIPR EEAAKRLDVL KRDVANACGF SL
//
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