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Database: UniProt
Entry: F5Z206_MYCSD
LinkDB: F5Z206_MYCSD
Original site: F5Z206_MYCSD 
ID   F5Z206_MYCSD            Unreviewed;       460 AA.
AC   F5Z206;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Phosphomannomutase PmmA {ECO:0000313|EMBL:AEF37006.1};
GN   Name=manB {ECO:0000313|EMBL:AEF37006.1};
GN   OrderedLocusNames=JDM601_3006 {ECO:0000313|EMBL:AEF37006.1};
OS   Mycolicibacter sinensis (strain JDM601) (Mycobacterium sinense).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacter.
OX   NCBI_TaxID=875328 {ECO:0000313|EMBL:AEF37006.1, ECO:0000313|Proteomes:UP000009224};
RN   [1] {ECO:0000313|EMBL:AEF37006.1, ECO:0000313|Proteomes:UP000009224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JDM601 {ECO:0000313|EMBL:AEF37006.1,
RC   ECO:0000313|Proteomes:UP000009224};
RX   PubMed=21685274; DOI=10.1128/JB.05291-11;
RA   Zhang Z.Y., Sun Z.Q., Wang Z.L., Wen Z.L., Sun Q.W., Zhu Z.Q., Song Y.Z.,
RA   Zhao J.W., Wang H.H., Zhang S.L., Guo X.K.;
RT   "Complete genome sequence of a novel clinical isolate, the nontuberculous
RT   Mycobacterium strain JDM601.";
RL   J. Bacteriol. 193:4300-4301(2011).
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; CP002329; AEF37006.1; -; Genomic_DNA.
DR   AlphaFoldDB; F5Z206; -.
DR   STRING; 875328.JDM601_3006; -.
DR   KEGG; mjd:JDM601_3006; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_9_2_11; -.
DR   OMA; KCSQVMY; -.
DR   Proteomes; UP000009224; Chromosome.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009224}.
FT   DOMAIN          3..118
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          152..252
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          263..366
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          371..449
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   460 AA;  47977 MW;  63DDBCABCC0C75E4 CRC64;
     MIKAYDVRGL VGSEIDESLV AEVGAAFARL MADEGARQVV IGHDMRDSSP PLSAAFAEGV
     IAQGLDVIRI GLASTDQLYF ASGSLDCPGA MFTASHNPAA YNGIKLCRAG AKPVGADSGL
     DRIRDELIAG VAPDAGRAGS RGAVSDRDVL ADYAAFLHSL VDISGGRPLR VAVDAGNGMA
     GHTAPAVFGS LRAITLLPLY FELDGNFPNH EANPLDPANL VDLQAFVRDS GADIGLAFDG
     DADRCFVVDE RGEPVSPSAV TGLVAARELA REPGATVIHN LITSRAVAEL VAERGGTPLR
     SRVGHSYIKA VMAETGAIFG GEHSAHYYFR DFWGADSGML AALHVLAALG EQQRPLSELT
     ADYQRYAASG EINYTLADGV DAQAYADAVV ASFGEQASVD HLDGVTVDLG GGSWFNLRSS
     NTEPLLRLNV EAPDSAAVDA VVGRVTEQVE AVTAAEKSRS
//
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