ID A0A024GV28_9STRA Unreviewed; 874 AA.
AC A0A024GV28;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Phosphomannomutase {ECO:0000256|ARBA:ARBA00012730, ECO:0000256|RuleBase:RU361118};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730, ECO:0000256|RuleBase:RU361118};
GN ORFNames=BN9_125600 {ECO:0000313|EMBL:CCI50591.1};
OS Albugo candida.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI50591.1, ECO:0000313|Proteomes:UP000053237};
RN [1] {ECO:0000313|EMBL:CCI50591.1, ECO:0000313|Proteomes:UP000053237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI50591.1,
RC ECO:0000313|Proteomes:UP000053237};
RA Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA Jones J.D.G.;
RT "Recombination and specialization in a pathogen metapopulation.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Enzyme with a broad specificity.
CC {ECO:0000256|ARBA:ARBA00003302}.
CC -!- FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol-
CC phosphate-mannose required for a number of critical mannosyl transfer
CC reactions. {ECO:0000256|RuleBase:RU361118}.
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|RuleBase:RU361118};
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 ECO:0000256|RuleBase:RU361118}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU361118}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU361118}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the eukaryotic PMM family.
CC {ECO:0000256|ARBA:ARBA00009736, ECO:0000256|RuleBase:RU361118}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCI50591.1}.
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DR EMBL; CAIX01000600; CCI50591.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024GV28; -.
DR STRING; 65357.A0A024GV28; -.
DR InParanoid; A0A024GV28; -.
DR OrthoDB; 46379at2759; -.
DR UniPathway; UPA00126; UER00424.
DR Proteomes; UP000053237; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00060; FHA; 1.
DR CDD; cd02585; HAD_PMM; 1.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 2.60.200.20; -; 2.
DR Gene3D; 3.30.1240.20; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR000253; FHA_dom.
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 InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR PANTHER; PTHR10466; PHOSPHOMANNOMUTASE; 1.
DR PANTHER; PTHR10466:SF0; PHOSPHOMANNOMUTASE; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF03332; PMM; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00240; FHA; 2.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 2.
DR PROSITE; PS50006; FHA_DOMAIN; 2.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU361118};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU361118};
KW Magnesium {ECO:0000256|PIRSR:PIRSR605002-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR605002-3};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000053237}.
FT DOMAIN 158..204
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 266..312
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 343..653
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 837
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT BINDING 849
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT BINDING 854
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
SQ SEQUENCE 874 AA; 98010 MW; ACC155316DF24A55 CRC64;
MAEEANPSNL FECQAISESQ SFKENKQSDE KDIENAIHSE MPSTLAKKTL GREDFDQRRR
STVIPFDISS FNSSRKAFTR ANTSGVNRFR NKDDASESLC ADGRSSNGVT KVQLQSSDGS
TEHVSTDKGP PWKHLILKMT AATDEDLITS FRFTDKGGGI GRDTENIASI PADKSLANRD
HALILHREDR FFLRNGNNQS GTYVRLTPCM MEEEKLQWPL LRDCSFRCGK SDFVVLSHDE
NAQTLELEAV SGKLAGAKFS IDCHGGGIGR STENVIHTGD GELSRKHAKI IFDDPTARFY
LYDLESTNGT YMRLCGPYDL PFRLESGDDL LISQTCLSVT HFDYGVHENM GARKYMEDTH
TVIQDLHIEC LTELGWHPQS YFGVFDGHGG VQASSFMEEQ LHVTIVGEFY RHRNVYETKA
PDAASAVISN LVKKQIVAAF ERTDKDFLKK SDRPQAGSTG TTVFIAGKRL FVANVGDSRT
ILSRSGEAVP LSNDHKPNRP DEAQRIRDIG GFVIHGRIMG ELAVSRAFGD APFKILDTPS
EPLIASGDAN IGSTLQKADV DSQLTINPSD ILKGPLVICT PEITETHLTD EEEFLVLASD
GLFDVLADQE VVDFVRAKLL QSRDVQRTTE ALVQHAIVHQ RSTDNVTAII TATNEMRERL
RRLKSQITIG VVGGSDLCKQ KEQLGEDVVN EFDYSFSENG LVAYHNGSLI GEKNLRDEYT
DAQLNRFLDY VLMYIASSQI PVKRGTFVEF RMGMINISPI GRNCSQKERD AFEQYDNIHH
VRKHFVEELK DKFADYNFAY SIGGQISFDV FPKGWDKTFC LQYIDPKAYD EIHFFGDKTQ
EGGNDYEIFH HERTIGHSVR SPEDTLRILD ELFP
//
