ID T2F4B5_LACLC Unreviewed; 252 AA.
AC T2F4B5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN ORFNames=kw2_0536 {ECO:0000313|EMBL:AGV72499.1};
OS Lactococcus cremoris subsp. cremoris KW2.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=1295826 {ECO:0000313|EMBL:AGV72499.1, ECO:0000313|Proteomes:UP000016704};
RN [1] {ECO:0000313|EMBL:AGV72499.1, ECO:0000313|Proteomes:UP000016704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KW2 {ECO:0000313|EMBL:AGV72499.1};
RX PubMed=24009606; DOI=10.3389/fmicb.2013.00257;
RA Kelly W.J., Altermann E., Lambie S.C., Leahy S.C.;
RT "Interaction between the genomes of Lactococcus lactis and phages of the
RT P335 species.";
RL Front. Microbiol. 4:257-257(2013).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR605002-3};
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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the eukaryotic PMM family.
CC {ECO:0000256|ARBA:ARBA00009736}.
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DR EMBL; CP004884; AGV72499.1; -; Genomic_DNA.
DR RefSeq; WP_011675578.1; NC_022369.1.
DR AlphaFoldDB; T2F4B5; -.
DR SMR; T2F4B5; -.
DR GeneID; 61108855; -.
DR KEGG; llw:kw2_0536; -.
DR PATRIC; fig|1295826.3.peg.514; -.
DR HOGENOM; CLU_065090_0_0_9; -.
DR UniPathway; UPA00126; UER00424.
DR Proteomes; UP000016704; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IEA:UniProt.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02585; HAD_PMM; 1.
DR Gene3D; 3.30.1240.20; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR005002; PMM.
DR InterPro; IPR043169; PMM_cap.
DR NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR PANTHER; PTHR10466; PHOSPHOMANNOMUTASE; 1.
DR PANTHER; PTHR10466:SF0; PHOSPHOMANNOMUTASE; 1.
DR Pfam; PF03332; PMM; 1.
DR SFLD; SFLDG01143; C2.B.3:_Phosphomannomutase_Lik; 1.
DR SFLD; SFLDG01140; C2.B:_Phosphomannomutase_and_P; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000313|EMBL:AGV72499.1};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|PIRSR:PIRSR605002-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR605002-3}.
FT ACT_SITE 8
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-1"
FT ACT_SITE 10
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-1"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
SQ SEQUENCE 252 AA; 28276 MW; 0C1F8FEEA53933C3 CRC64;
MKKILSFDID NTLNEPKMPI FPEMAELLAT LSQKYIIAPI SGQKYDQFLI QIINNLPESA
NLDNFHLFVA QGTQYYAHKA GEWKQVFNYA LTDEQANAIM GALEKAAKEL GHWDESVLLP
GDEINENRES MIAYSAIGQK AGVEAKQAWD PDMTKRNEIA KLASQYAPEF EFEVAGTTTI
NGFVPGQNKE FGMNHLMEEL NVTKEEILYF GDMTQPGGND YPVVQMGIET ITVRDWKETA
AILKAIIAME EA
//