ID Q2YK25_BRUA2 Unreviewed; 477 AA.
AC Q2YK25;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase:Phosphogluc omutase/phosphomannomutase C terminal:Phosphoglucomutase/phosphomannomutase {ECO:0000313|EMBL:CAJ13021.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:CAJ13021.1};
GN OrderedLocusNames=BAB2_0855 {ECO:0000313|EMBL:CAJ13021.1};
OS Brucella abortus (strain 2308).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391 {ECO:0000313|EMBL:CAJ13021.1, ECO:0000313|Proteomes:UP000002719};
RN [1] {ECO:0000313|EMBL:CAJ13021.1, ECO:0000313|Proteomes:UP000002719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308 {ECO:0000313|EMBL:CAJ13021.1,
RC ECO:0000313|Proteomes:UP000002719};
RX PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005;
RG Microbial Genomics Group;
RG Lawrence Livermore National Laboratory;
RG and the Genome Analysis Group;
RG Oak Ridge National Laboratory;
RA Chain P., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
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}.
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DR EMBL; AM040265; CAJ13021.1; -; Genomic_DNA.
DR RefSeq; WP_002966241.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YK25; -.
DR SMR; Q2YK25; -.
DR STRING; 359391.BAB2_0855; -.
DR GeneID; 3828093; -.
DR KEGG; bmf:BAB2_0855; -.
DR PATRIC; fig|359391.11.peg.545; -.
DR HOGENOM; CLU_045514_1_0_5; -.
DR PhylomeDB; Q2YK25; -.
DR Proteomes; UP000002719; Chromosome II.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03088; ManB; 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 PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 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 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, ECO:0000313|EMBL:CAJ13021.1};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002719}.
FT DOMAIN 6..136
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 158..255
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 272..371
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 411..461
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 477 AA; 50612 MW; BDA62CB76742CBB4 CRC64;
MSSNSLKFGT SGLRGLAVEL NGLPAYAYTM AFVQMLAAKG QLQKGDKVFV GRDLRPSSPD
IAALAMGAIE DAGFTPVNCG VLPTPALSYY AMGAKAPSIM VTGSHIPDDR NGLKFYRRDG
EIDKDDEAAI SAAYRKLPAI LAARKHVGST ETDAALQAYA DRYAGFLGKG SLNGLRVGVY
QHSSVARDLL MYLLTTLGVE PVALGRSDIF VPVDTEALRP EDIALLAQWG KSDRLDAIVS
TDGDADRPLI ADEHGQFVRG DLAGAITATW VGADTLVTPV TSNTALESRF PKVLRTRVGS
PYVIASMAQV STGNSGPVIG FEANGGVLLG STVERNGRSL TALPTRDALL PILACLATVH
EKKTPLSTIA RSYGFRVALS DRLQNIPQEA STAFLALLED ADKRASLFPA GDAIVRVETI
DGVKLFFQSG NAVHYRASGN APELRCYVES SDDTQAAKLQ ALGLEIARKA LKDATRP
//
