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Database: UniProt
Entry: T2F4B5_LACLC
LinkDB: T2F4B5_LACLC
Original site: T2F4B5_LACLC 
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
//
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