ID L5L9I7_9MOLU Unreviewed; 560 AA.
AC L5L9I7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase, C-terminal domain protein {ECO:0000313|EMBL:ELK20095.1};
GN ORFNames=D500_0478 {ECO:0000313|EMBL:ELK20095.1};
OS Mycoplasma feriruminatoris.
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=1179777 {ECO:0000313|EMBL:ELK20095.1};
RN [1] {ECO:0000313|EMBL:ELK20095.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G5847 {ECO:0000313|EMBL:ELK20095.1};
RX PubMed=23469346;
RA Fischer A., Santana-Cruz I., Giglio M., Nadendla S., Drabek E., Vilei E.M.,
RA Frey J., Jores J.;
RT "Genome Sequence of Mycoplasma feriruminatoris sp. nov., a Fast-Growing
RT Mycoplasma Species.";
RL Genome Announc. 1:E00216-12(2013).
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:ELK20095.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ANFU01000024; ELK20095.1; -; Genomic_DNA.
DR RefSeq; WP_008363470.1; NZ_KB199594.1.
DR AlphaFoldDB; L5L9I7; -.
DR STRING; 1179777.D500_0478; -.
DR PATRIC; fig|1179777.3.peg.445; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_0_0_14; -.
DR OrthoDB; 9806956at2; -.
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}.
FT DOMAIN 43..185
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 208..312
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 321..448
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 497..534
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 560 AA; 64125 MW; C67E083AE7061654 CRC64;
MSFNKLDQTY LNWINHPNLD QELKELLNKA DDNELNAAFN LELKFGTAGI RGILGAGPGR
FNVYTIKKVT IAYAKLLQSK YSYDLNKGVV IGHDNRHNSK KFAQLVANIL TSFNIKAYLF
KNNDLQPTPV VSFATKALNC IGGVVITASH NPAEYNGYKI YDPYGCQLMP NDTDVIAEEM
NKIENILDWT FEPNNNLLEI VDQTIIDKYF EMIQNLEFYK NQQESKSKLK IIYSAVNGTG
SLYTPIVLKQ SGYEVIEVQE HSFEDETFKN VVNPNPEFDP AWKIPLQYAK KYDADIIILN
DPDADRFGMA IKHNNEFVRL NGNQTGAILI DWKLSNLKRL NKLPKNPALY SSFVTSDLGD
RIASETYNSV VVKTLTGFKW MGQEMLKEPL NGLNFVFAYE ESYGYVIDDS TRDKDGIQAS
ITAAEACWYY KNQNLTLVDY LNQLYEKYGY YYTTTFNLNF KPEEKDSKIA PIMKLLRTTG
INQINNLKVI KIEDYINGLY NMPSEDLIKI YLEDKSWIAI RPSGTEPKLK IYFVIVDSSL
QKAENKAEMI YKELKTILNI
//
