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Database: UniProt
Entry: A0A095YVV7_9ACTO
LinkDB: A0A095YVV7_9ACTO
Original site: A0A095YVV7_9ACTO 
ID   A0A095YVV7_9ACTO        Unreviewed;       558 AA.
AC   A0A095YVV7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:KGF00334.1};
GN   ORFNames=HMPREF1627_05905 {ECO:0000313|EMBL:KGF00334.1};
OS   Actinomyces sp. S6-Spd3.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=1284680 {ECO:0000313|EMBL:KGF00334.1, ECO:0000313|Proteomes:UP000029604};
RN   [1] {ECO:0000313|EMBL:KGF00334.1, ECO:0000313|Proteomes:UP000029604}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S6-Spd3 {ECO:0000313|EMBL:KGF00334.1,
RC   ECO:0000313|Proteomes:UP000029604};
RA   McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA   Sutton G., Nelson K.E.;
RL   Submitted (JUL-2014) 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}.
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:KGF00334.1}.
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DR   EMBL; JRMV01000276; KGF00334.1; -; Genomic_DNA.
DR   RefSeq; WP_034501832.1; NZ_JRMV01000276.1.
DR   AlphaFoldDB; A0A095YVV7; -.
DR   PATRIC; fig|1284680.3.peg.911; -.
DR   eggNOG; COG1109; Bacteria.
DR   Proteomes; UP000029604; 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; 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; IPR005841; Alpha-D-phosphohexomutase_SF.
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   PRINTS; PR00509; PGMPMM.
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:UP000029604}.
FT   DOMAIN          50..166
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          213..318
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          330..437
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          495..535
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   558 AA;  58852 MW;  CA4E36F607625F52 CRC64;
     MNVIERAQQW VDHDPDPATA AELASAVEAA RAGDESALAE LNRAMNGPLQ FGTAGLRGEI
     GPGESRMNLS VVIRATAGLC AVLLRHATRA PRVVIGCDAR YGSVDFAHAA ARVASAAGCE
     VFLLPLKNPT PLTAFSVREL DADAGIMVTA SHNPPRDNGY KVYLGGTVVT GAGQGVQIVS
     PFDAEIASAI ASAPFADQIA QNDELIVNVD PREDYIARAA SLAQGSPEIK EDLAITLTAM
     HGVGAALTQQ VLNEAGFTNV SLVAEQVEPD PDFPTVSFPN PEEPGALDLA IAHARAHASD
     LIIAVDPDAD RCALAVPDEA SSNGWRQLSG DETGSLLGEF LAGSAPEDAV FANSIVSSRL
     LGKIAQGHGL KYQHTLTGFK WIARVPGLYF GYEEAIGFCP DPTRVRDKDG IATSVVAASL
     FAMLKSQGRT AKDELERMAR LYGLHVTAPL TFRVDRLELI AEGMQRLRSQ PPTTLAGAEV
     EGVVDLSKGW DGLPGTDALM VTTTAGDRVI ARPSGTEPKL KCYLEVVIPV EEGAEVPWAQ
     ARERLETIKS EFGAAIGI
//
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