ID B5L3L6_ECOLX Unreviewed; 462 AA.
AC B5L3L6;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Phosphomannomutase {ECO:0000256|ARBA:ARBA00021706};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN Name=manB {ECO:0000313|EMBL:ACA24886.1};
GN Synonyms=cpsG {ECO:0000313|EMBL:NEM87157.1};
GN ORFNames=G3V95_16930 {ECO:0000313|EMBL:NEM87157.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ACA24886.1};
RN [1] {ECO:0000313|EMBL:ACA24886.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18422615; DOI=10.1111/j.1574-6976.2008.00114.x;
RA Liu B., Knirel Y.A., Feng L., Perepelov A.V., Senchenkova S.N., Wang Q.,
RA Reeves P.R., Wang L.;
RT "Structure and genetics of Shigella O antigens.";
RL FEMS Microbiol. Rev. 32:627-653(2008).
RN [2] {ECO:0000313|EMBL:NEM87157.1, ECO:0000313|Proteomes:UP000469708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8375wC2 {ECO:0000313|EMBL:NEM87157.1,
RC ECO:0000313|Proteomes:UP000469708};
RA Subbiah M., Call D.;
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU294175; ACA24886.1; -; Genomic_DNA.
DR EMBL; JAAGYI010000028; NEM87157.1; -; Genomic_DNA.
DR RefSeq; WP_032214185.1; NZ_WSPY01000008.1.
DR Proteomes; UP000469708; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:NEM87157.1};
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}.
FT DOMAIN 13..137
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 159..264
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 269..378
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 384..451
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 462 AA; 51146 MW; D6A1A3AF05E7F985 CRC64;
MHNKIILDKL TCFKAYDIRG KLGEELNEDI AWRIGRAYGE FLKPKTIVLG GDVRLTSETL
KLALAKGLQD AGVDVLDIGM SGTEEIYFAT FHLGVDGGIE VTASHNPMDY NGMKLVREGA
RPISGDTGLR DVQRLAEAND FPPVDETKRG RYQQINLRDA YVDHLFGYIN VKNLTPLKLV
INSGNGAAGP VVDAIEARFK ALGAPVELIK VHNTPDGNFP NGIPNPLLPE CRDDTRNAVI
KHGADMGIAF DGDFDRCFLF DEKGQFIEGY YIVGLLAEAF LEKNPGAKII HDPRLSWNTV
DVVTAAGGTP VMSKTGHAFI KERMRKEDAI YGGEMSAHHY FRDFAYCDSG MIPWLLVAEL
VCLKGKTLGE LVRDRMAAFP ASGEINSKLA HPVEAINRVE QHFSREALAV DRTDGISMTF
ADWRFNLRSS NTEPVVRLNV ESRGDVPLME EKTKLILELL NK
//
