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
//