ID A0A1T4P7D9_9PORP Unreviewed; 463 AA.
AC A0A1T4P7D9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:SJZ87414.1};
GN ORFNames=SAMN02745171_01363 {ECO:0000313|EMBL:SJZ87414.1};
OS Porphyromonas circumdentaria.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=29524 {ECO:0000313|EMBL:SJZ87414.1, ECO:0000313|Proteomes:UP000190121};
RN [1] {ECO:0000313|Proteomes:UP000190121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51356 {ECO:0000313|Proteomes:UP000190121};
RA Varghese N., Submissions S.;
RL Submitted (FEB-2017) 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; FUXE01000014; SJZ87414.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4P7D9; -.
DR STRING; 29524.SAMN02745171_01363; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000190121; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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 InterPro; IPR024086; GlmM_arc-type.
DR NCBIfam; TIGR03990; Arch_GlmM; 1.
DR PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 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}.
FT DOMAIN 8..142
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 170..263
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 270..376
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 395..458
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 463 AA; 50106 MW; 10E8B34FF38ABE62 CRC64;
MSLIKSISGI RGTIGGSVQE GLNPLSITRF TAAYATFIKK QSGLEKPLIV VGRDARISGD
MVRRIVTGTL VAIGCDVIDI DLATTPTTEM AVIGYKAQGG IIITASHNPK QWNALKLLGG
NGEFLSDAEG RAVLAIAEEE AFTYVTVENM GVVTSGDYLE AHCQKILELE EVDVEAIRTA
GFRVAFDSIN SVGGIAVPYL LRKLGVEVIF PLFDEPTGDF AHNPEPLPHH LTELSDTVRT
NRADVGFSVD PDVDRLAIID EKGDPFGEEY TLVAVADYLL EFHGGGNTVS NLSSTRALRD
VTERNGRGVY SAAAVGEVNV VTKMKETSAL IGGEGNGGVI FPKLHAGRDA LLGIALFLTL
LAKKKKSVSA LRAEYPDYFM SKQRADLPEA TDVRALLHEV EKLYAEHTPN TIDGVKIDFE
SSWVHIRPSN TEPIIRIYTE ASSQEAADHL ADRFREVVLS LLK
//
