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Database: UniProt
Entry: L7V7P8_MYCL1
LinkDB: L7V7P8_MYCL1
Original site: L7V7P8_MYCL1 
ID   L7V7P8_MYCL1            Unreviewed;       466 AA.
AC   L7V7P8;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Phosphomannomutase PmmA {ECO:0000313|EMBL:AGC61404.1};
DE            EC=5.4.2.8 {ECO:0000313|EMBL:AGC61404.1};
GN   Name=pmmA {ECO:0000313|EMBL:AGC61404.1};
GN   OrderedLocusNames=MULP_01445 {ECO:0000313|EMBL:AGC61404.1};
OS   Mycobacterium liflandii (strain 128FXT).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=459424 {ECO:0000313|EMBL:AGC61404.1, ECO:0000313|Proteomes:UP000011157};
RN   [1] {ECO:0000313|EMBL:AGC61404.1, ECO:0000313|Proteomes:UP000011157}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=128FXT {ECO:0000313|EMBL:AGC61404.1,
RC   ECO:0000313|Proteomes:UP000011157};
RX   PubMed=23204453; DOI=10.1128/JB.02132-12;
RA   Tobias N.J., Doig K.D., Medema M.H., Chen H., Haring V., Moore R.,
RA   Seemann T., Stinear T.P.;
RT   "Complete Genome Sequence of the Frog Pathogen Mycobacterium ulcerans
RT   Ecovar Liflandii.";
RL   J. Bacteriol. 195:556-564(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}.
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DR   EMBL; CP003899; AGC61404.1; -; Genomic_DNA.
DR   RefSeq; WP_012393155.1; NC_020133.1.
DR   AlphaFoldDB; L7V7P8; -.
DR   KEGG; mli:MULP_01445; -.
DR   PATRIC; fig|459424.11.peg.1480; -.
DR   HOGENOM; CLU_016950_9_2_11; -.
DR   Proteomes; UP000011157; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd03089; PMM_PGM; 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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
DR   PANTHER; PTHR43771:SF1; PHOSPHOMANNOMUTASE; 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.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AGC61404.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          12..134
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          167..260
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          272..374
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          379..455
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   466 AA;  48916 MW;  DE2A41EADCF342A9 CRC64;
     MSWPAAVINR VIKAYDVRGL VGEEITEALC ADIGAAFARL MRGEGARQVV IGYDMRDSSP
     ALAAAFASGV VAQGLDVVRI GLASTDQLYF AAGQLDCPGA MFTASHNPAA YNGIKLCRAG
     AKPVGADTGL NAIREDLVNP VAIAVAETAG TIADKDVLGD YGVFLRSLVN TADLRPLRVA
     VDAGNGMAGH TAPAVLGAID SVTLLPLYFE LDGTFPNHEA NPLDPANLLD LQKFVVATGA
     DIGLAFDGDA DRCFVVDERG EPVSPSTVTS LVAARELSRE IGATVIHNVI TSRAVPELVV
     ERGGTPLRSR VGHSYIKALM ADTGAIFGGE HSAHYYFRDF WGADSGMLAA LYVLAALGEQ
     SRPLSELTAD YQRYASSGEI NFTVADAPAC VEGVLKSFGS RIVSIDHLDG VTVDLGDDSW
     FNLRSSNTEP LLRLNVEARS AEDVDAVVQQ VSAEIAAQSP RGEAGP
//
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