ID Q9ETP1_SALBN Unreviewed; 456 AA.
AC Q9ETP1;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 24-JAN-2024, entry version 87.
DE RecName: Full=Phosphomannomutase {ECO:0000256|ARBA:ARBA00021706};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN Name=manB {ECO:0000313|EMBL:AAG41710.1};
OS Salmonella bongori.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=54736 {ECO:0000313|EMBL:AAG41710.1};
RN [1] {ECO:0000313|EMBL:AAG41710.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11238967;
RA Jensen S.O., Reeves P.R.;
RT "Molecular evolution of the GDP-mannose pathway genes (manB and manC) in
RT Salmonella enterica.";
RL Microbiology 147:599-610(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate;
CC Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735;
CC EC=5.4.2.8; Evidence={ECO:0000256|ARBA:ARBA00000586};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC step 2/2. {ECO:0000256|ARBA:ARBA00004699}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
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DR EMBL; AY012160; AAG41709.1; -; Genomic_DNA.
DR EMBL; AY012161; AAG41710.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9ETP1; -.
DR SMR; Q9ETP1; -.
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; 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; IPR016066; A-D-PHexomutase_CS.
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.
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 7..126
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 153..258
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 263..373
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 378..439
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 456 AA; 49907 MW; 9FEC2470182A512C CRC64;
MNKLTCFKAY DIRGRLGEEL NEDIAWRIGR AYGEYLKPKT IVLGGDVRLT SESLKLALAK
GLQDAGVDVL DIGVSGTEEI YFATFHLGVD GGIEVTASHN PMDYNGMKLV REGARPISGD
TGLRDVQRLA EADDFPPVNE AARGSYRQIS LRDAYIDHLL GYISVSNLTP LKLVVNAGNG
AAGPVVDAIE ARLKALGAPV EFIKIHNTPD GTFPNGIPNP LLPECRGDTR NAVIEHGADM
GIAFDGDFDR CFLFDEKGQF IEGYYIVGLL AEAFLEKHPG AKIIHDPRLT WNTEAVVTAA
GGTPVMSKTG HAFIKERMRA EDAIYGGEMS AHHYFRDFAY CDSGMIPWLL VAELVCLKGQ
SLGELVRDRM AAYPASGEIN SRLAEPAEAI ARVEAYFAEE AQAVDRTDGL SMSFPDWRFN
LRSSNTEPVV RLNVESRGDI PLMEARTRTL LALLNQ
//
