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Database: UniProt
Entry: K1R8K0_CRAGI
LinkDB: K1R8K0_CRAGI
Original site: K1R8K0_CRAGI 
ID   K1R8K0_CRAGI            Unreviewed;       530 AA.
AC   K1R8K0;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 46.
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=CGI_10018115 {ECO:0000313|EMBL:EKC37500.1};
OS   Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX   NCBI_TaxID=29159 {ECO:0000313|EMBL:EKC37500.1};
RN   [1] {ECO:0000313|EMBL:EKC37500.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC37500.1};
RX   PubMed=22992520; DOI=10.1038/nature11413;
RA   Zhang G., Fang X., Guo X., Li L., Luo R., Xu F., Yang P., Zhang L.,
RA   Wang X., Qi H., Xiong Z., Que H., Xie Y., Holland P.W., Paps J., Zhu Y.,
RA   Wu F., Chen Y., Wang J., Peng C., Meng J., Yang L., Liu J., Wen B.,
RA   Zhang N., Huang Z., Zhu Q., Feng Y., Mount A., Hedgecock D., Xu Z., Liu Y.,
RA   Domazet-Loso T., Du Y., Sun X., Zhang S., Liu B., Cheng P., Jiang X.,
RA   Li J., Fan D., Wang W., Fu W., Wang T., Wang B., Zhang J., Peng Z., Li Y.,
RA   Li N., Wang J., Chen M., He Y., Tan F., Song X., Zheng Q., Huang R.,
RA   Yang H., Du X., Chen L., Yang M., Gaffney P.M., Wang S., Luo L., She Z.,
RA   Ming Y., Huang W., Zhang S., Huang B., Zhang Y., Qu T., Ni P., Miao G.,
RA   Wang J., Wang Q., Steinberg C.E., Wang H., Li N., Qian L., Zhang G., Li Y.,
RA   Yang H., Liu X., Wang J., Yin Y., Wang J.;
RT   "The oyster genome reveals stress adaptation and complexity of shell
RT   formation.";
RL   Nature 490:49-54(2012).
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}.
CC   -!- SIMILARITY: Belongs to the eukaryotic PMM family.
CC       {ECO:0000256|ARBA:ARBA00009736, ECO:0000256|RuleBase:RU361118}.
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DR   EMBL; JH818095; EKC37500.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1R8K0; -.
DR   HOGENOM; CLU_514147_0_0_1; -.
DR   InParanoid; K1R8K0; -.
DR   UniPathway; UPA00126; UER00424.
DR   GO; GO:0005737; C:cytoplasm; 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: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:SF14; PHOSPHOMANNOMUTASE; 1.
DR   Pfam; PF03332; PMM; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU361118};
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}.
FT   BINDING         491
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT   BINDING         503
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT   BINDING         505
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT   BINDING         508
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
SQ   SEQUENCE   530 AA;  59491 MW;  FC8FC10C5E4F1E5A CRC64;
     MATKRPCLRK STRAQSKTKE VNGEDPSKVD NDKLSEPIPK TQTRRITKLK KHVTEKPEII
     NIDEESEHGD GSFISQIIPS CEKDTFLCSQ DTSAEVFWDC TSPDMRKIIR SRHRRDKHLK
     SNVVDIVQTL STTSDVDTED LEDKSKNGLL GLWMDSDAPD ISSKFTATNL TSFSPTNSFP
     PQRAQKEKRE ATDTLSSVLQ EKLSMRIKKE RSPLGTKIRS SAEKRKRSSL SGVTESSSKI
     SKVERNEGKA CALPEEVEKL SETSWSEDDF YEEDSFIIRA TQAPGELANK CETKTSSNKE
     VNNKAAPQDM LDFLKKLKQK CIVGLVGGSD LSKIAEQMGR DVVNEYDYVF SENGLVAYKE
     GKQIGQENLL HNKGEECLQK VINFALKYMS ELQLPAKRGT FVEFRSSMLN LCPVGRSCSQ
     KERDEFAAFD KENNIRKKFV EALYKNFPEA GLKFAIGGQI SIDVFPTGWD KTFCLQFLEK
     DGIKTIHFFG DKTTAGGNDH EIYEDSRTIG HSVTDPSDTI KQVSAIIPGL
//
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