ID C7LAK1_BRUMC Unreviewed; 445 AA.
AC C7LAK1;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:ACU47536.1};
GN Name=manB {ECO:0000313|EMBL:ACU47536.1};
GN OrderedLocusNames=BMI_I536 {ECO:0000313|EMBL:ACU47536.1};
OS Brucella microti (strain CCM 4915).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=568815 {ECO:0000313|EMBL:ACU47536.1, ECO:0000313|Proteomes:UP000002188};
RN [1] {ECO:0000313|EMBL:ACU47536.1, ECO:0000313|Proteomes:UP000002188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 4915 {ECO:0000313|EMBL:ACU47536.1,
RC ECO:0000313|Proteomes:UP000002188};
RX PubMed=19653890; DOI=10.1186/1471-2164-10-352;
RA Audic S., Lescot M., Claverie J.-M., Scholz H.C.;
RT "Brucella microti: the genome sequence of an emerging pathogen.";
RL BMC Genomics 10:352-352(2009).
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; CP001578; ACU47536.1; -; Genomic_DNA.
DR AlphaFoldDB; C7LAK1; -.
DR KEGG; bmr:BMI_I536; -.
DR HOGENOM; CLU_045514_1_0_5; -.
DR Proteomes; UP000002188; Chromosome 1.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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};
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}.
FT DOMAIN 6..99
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 132..229
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 233..349
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 361..441
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 445 AA; 48468 MW; 314EA62270A71833 CRC64;
MVYVSAFLQH LSHNFSYETV YVGADLRESS PKITISCYRA IELTGRRAIW AGNVPTPALA
AYAMARNAPA IMITGSHIPE AYNGIKFYRP DGEFLKDDEA PVRGLAEELL SKVVDGQRSV
NLPAPLADVA EEYVSRSIGA FGRDTLAGMK IGIDLHSAVG RDILVRIFKG LGAEVYPFRR
TENFVAVDTE ALDPADISRA RTFIAEHGLD AVVSTDGDGD RPLVIDDQGR QVNGDTLGIL
TARYLRAKTV VTPLSTTSAL EESGWFENIH RTRIGSPYVV VEMARAVAHP VVGFEANGGF
LLGDDVALKT GLLRRLPTRD AVLPAVAVLA QAKDQGMRLS EMVATLPSRF MKADRVKEVP
GDRAAPFLHA IETSQSFRSN FSPLIAEPEA ISTVDGVRMA FANGDTVHFR QSGNAPEMRI
YIETDSAEKT DRMLSEFIAK LSETI
//
