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Database: UniProt
Entry: A0A095X7H5_9ACTO
LinkDB: A0A095X7H5_9ACTO
Original site: A0A095X7H5_9ACTO 
ID   A0A095X7H5_9ACTO        Unreviewed;       563 AA.
AC   A0A095X7H5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:KGF06055.1};
GN   ORFNames=HMPREF1631_04500 {ECO:0000313|EMBL:KGF06055.1};
OS   Arcanobacterium sp. S3PF19.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Arcanobacterium.
OX   NCBI_TaxID=1219585 {ECO:0000313|EMBL:KGF06055.1, ECO:0000313|Proteomes:UP000054502};
RN   [1] {ECO:0000313|EMBL:KGF06055.1, ECO:0000313|Proteomes:UP000054502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S3PF19 {ECO:0000313|EMBL:KGF06055.1,
RC   ECO:0000313|Proteomes:UP000054502};
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:KGF06055.1}.
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DR   EMBL; JRMX01000013; KGF06055.1; -; Genomic_DNA.
DR   RefSeq; WP_034232673.1; NZ_JRMX01000013.1.
DR   AlphaFoldDB; A0A095X7H5; -.
DR   STRING; 1219585.HMPREF1631_04500; -.
DR   eggNOG; COG1109; Bacteria.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000054502; 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:UP000054502}.
FT   DOMAIN          51..192
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          217..316
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          328..441
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          490..526
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   563 AA;  60289 MW;  7A310B7875713EE5 CRC64;
     MKINTTEIEE WIAHDPQEET RAELSSLLAR AKDGDTAAKD SLADRFRGPL QFGTAGLRGK
     MGAGPFRMNR AVVRRAAAGL TAWLKEKIGS DALVVIGYDA RYNSADFAKD TAAIVTAAGL
     RAKIMPRTLP TPLLAFAVRH LHADAGVMVT ASHNPAQDNG YKVYVGNRAV DADGNGVQII
     PPTDGEIAAK IAAAPHADEI PLAESGWEEI EETVIETYIR NTVEKLGRTG ARDLKIVYTA
     MHGVGYETMM KIFAGAGFTD VTGVPEQIAP DPDFPTVAFP NPEEAGALDL AIALAEKENA
     DIVIASDPDA DRCSAAVPTA EGWRQLSGDE IGSVLGEIAA RRNAGKGREA TLASSVVSSR
     LLEQIARHHG LHYQATLTGF KWIARAPKIV YGYEEAIGFC VNPADVKDKD GISAGLALAV
     EAARLKAEGR SMTDALDDLY RRHGVYLSGP VTVRVEDLSI IPATMAKLRT CPPTVLAGSK
     VVRFEDLSKG SAKLPPTDAV KIVTEANDRV IVRPSGTEPK VKCYLEVIVP LKPEDEGGLR
     AAKTEAAKRL SFFKQDMHEA LKL
//
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