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Database: UniProt
Entry: R7WJB3_9NOCA
LinkDB: R7WJB3_9NOCA
Original site: R7WJB3_9NOCA 
ID   R7WJB3_9NOCA            Unreviewed;       459 AA.
AC   R7WJB3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:EOM75376.1};
GN   ORFNames=Rrhod_3174 {ECO:0000313|EMBL:EOM75376.1};
OS   Rhodococcus rhodnii LMG 5362.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1273125 {ECO:0000313|EMBL:EOM75376.1, ECO:0000313|Proteomes:UP000013525};
RN   [1] {ECO:0000313|EMBL:EOM75376.1, ECO:0000313|Proteomes:UP000013525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 5362 {ECO:0000313|EMBL:EOM75376.1,
RC   ECO:0000313|Proteomes:UP000013525};
RX   PubMed=23788540;
RA   Pachebat J.A., van Keulen G., Whitten M.M., Girdwood S., Del Sol R.,
RA   Dyson P.J., Facey P.D.;
RT   "Draft Genome Sequence of Rhodococcus rhodnii Strain LMG5362, a Symbiont of
RT   Rhodnius prolixus (Hemiptera, Reduviidae, Triatominae), the Principle
RT   Vector of Trypanosoma cruzi.";
RL   Genome Announc. 1:e00329-13(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}.
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:EOM75376.1}.
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DR   EMBL; APMY01000095; EOM75376.1; -; Genomic_DNA.
DR   RefSeq; WP_010839207.1; NZ_APMY01000095.1.
DR   AlphaFoldDB; R7WJB3; -.
DR   PATRIC; fig|1273125.3.peg.3016; -.
DR   eggNOG; COG1109; Bacteria.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000013525; Unassembled WGS sequence.
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:UP000013525}.
FT   DOMAIN          12..128
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          159..259
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          265..371
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          378..454
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   459 AA;  48491 MW;  C20D18A84FF6F88B CRC64;
     MSRSAESVHS VVKAYDVRGL VGEQLDEGFV RDLGGAFAHL MRSEGAARVA VGHDMRDSSP
     TLAHAFAEGV TAQGLDVVLL GLTSTDELYF ASGRLECPGA MFTASHNPAR YNGVKMCRAF
     AKPVGQQTGL ADIAQQLVDG VAPYDGARGD IAEADLLADY AEFLRSLVDL SELRPTRIVV
     DAGNGMGGMT APAVFGPLAA VTIDPLYFEL DGTFPNHEAN PLDPANLVDL SARVRETGAD
     LGLAFDGDAD RCFVVDEKGD VVSPSAITAL VAQHALAAEP GATIIYNAIT SRAVPELVEE
     WGGVAVRTRV GHSFIKQQMS ETGAVFGGEH SGHYYFRDFW NADSGMLAAL HVLAAYGAQD
     RPLSELMAEY VKYADSGEIN STVDDLAAAA DEVVAAFAER TVAVDTLDGV TVDLGDHTWF
     NLRPSNTEPL LRLNAEAPSR GAVDAVVGEI LGIVRGRLG
//
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