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
//