ID A0A0F7JVJ3_9SPHN Unreviewed; 248 AA.
AC A0A0F7JVJ3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN ORFNames=NX02_p0285 {ECO:0000313|EMBL:AKH18698.1};
OS Sphingomonas sanxanigenens DSM 19645 = NX02.
OG Plasmid pNXO2 {ECO:0000313|EMBL:AKH18698.1,
OG ECO:0000313|Proteomes:UP000018851}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1123269 {ECO:0000313|EMBL:AKH18698.1, ECO:0000313|Proteomes:UP000018851};
RN [1] {ECO:0000313|EMBL:AKH18698.1, ECO:0000313|Proteomes:UP000018851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NX02 {ECO:0000313|EMBL:AKH18698.1,
RC ECO:0000313|Proteomes:UP000018851};
RC PLASMID=Plasmid pNXO2 {ECO:0000313|Proteomes:UP000018851};
RA Huang H., Ma T.;
RT "Plasmid of Sphingomonas sanxanigenens NX02.";
RL Submitted (MAY-2015) 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; CP011450; AKH18698.1; -; Genomic_DNA.
DR RefSeq; WP_047100272.1; NZ_CP011450.1.
DR AlphaFoldDB; A0A0F7JVJ3; -.
DR KEGG; ssan:NX02_p0285; -.
DR OrthoDB; 2241234at2; -.
DR UniPathway; UPA00126; UER00424.
DR Proteomes; UP000018851; Plasmid pNXO2.
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 SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000313|EMBL:AKH18698.1};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|PIRSR:PIRSR605002-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR605002-3};
KW Plasmid {ECO:0000313|EMBL:AKH18698.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018851}.
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 208
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
SQ SEQUENCE 248 AA; 27073 MW; 83B98DDC7EFF9476 CRC64;
MKQLMAFDLD GTLAESKAPL DDEVAGLLAA LLSFAQVAVI SGGDWPQFKK QVVDRLPPGA
ELGRLWILPT AGAKLFRFAG EWRQAYSEAI TPAEKAHILK ELDRAIKAAG LDRDPAWGPR
IEDRGTQITY SGIGQKAPLE AKEAWDPDRR KRLQLQEMLR RTLTEWSVNI GGTTSIDITR
AGIDKGFGLR KLAAESGVPL EDMVFLGDSI FPGGNDYPAV TVGVDAVAVR DVQETKSILH
ALTLWLGR
//
