ID W6EXT3_BIFBR Unreviewed; 267 AA.
AC W6EXT3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN ORFNames=B7019_0717 {ECO:0000313|EMBL:AHJ19009.1};
OS Bifidobacterium breve JCM 7019.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1385940 {ECO:0000313|EMBL:AHJ19009.1, ECO:0000313|Proteomes:UP000019336};
RN [1] {ECO:0000313|EMBL:AHJ19009.1, ECO:0000313|Proteomes:UP000019336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 7019 {ECO:0000313|EMBL:AHJ19009.1,
RC ECO:0000313|Proteomes:UP000019336};
RA Bottacini F.;
RT "The Bifidobacterium breve pan-genome.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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; CP006713; AHJ19009.1; -; Genomic_DNA.
DR RefSeq; WP_025221424.1; NZ_CP006713.1.
DR AlphaFoldDB; W6EXT3; -.
DR KEGG; bbrc:B7019_0717; -.
DR PATRIC; fig|1385940.3.peg.739; -.
DR HOGENOM; CLU_065090_0_0_11; -.
DR UniPathway; UPA00126; UER00424.
DR Proteomes; UP000019336; 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 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 Pfam; PF03332; PMM; 1.
DR SFLD; SFLDG01143; C2.B.3:_Phosphomannomutase_Lik; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|PIRSR:PIRSR605002-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR605002-3}.
FT ACT_SITE 24
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-1"
FT ACT_SITE 26
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-1"
FT BINDING 24
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT BINDING 26
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
SQ SEQUENCE 267 AA; 28969 MW; F74F440AC647CC83 CRC64;
MVVRSWAELD LDDICAHARV FGFDLDNTLA SSKQPMEPAM IARFSALTAH ATVALISGGG
MDVVTSQVLD VLGPDADRGH LHVMPTSGSR YYRWDGERWT LVYAHDLDDR TVAAITSSLE
RHAKELGMWE EHVWGNRIEN RGSQITFSAL GQYAPVAAKQ SWDPDNIKKR ALVEAVKADL
PDLRVRSGGY SSVDVSQHGI DKAYAVRRLA EILDVPVGGI VFIGDRMTPD GNDYPAVAAG
AVGMKVENPE DALGLMDALL QRVGASA
//
