ID Q0VC17_BOVIN Unreviewed; 262 AA.
AC Q0VC17;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 123.
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 Name=PMM1 {ECO:0000313|EMBL:AAI20395.1,
GN ECO:0000313|Ensembl:ENSBTAP00000005231.3,
GN ECO:0000313|VGNC:VGNC:33072};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|EMBL:AAI20395.1};
RN [1] {ECO:0000313|EMBL:AAI20395.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=L1 Hereford {ECO:0000313|EMBL:AAI20395.1};
RC TISSUE=Basal ganglia {ECO:0000313|EMBL:AAI20395.1};
RA Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA Holt R., Jones S.J., Marra M.A.;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000005231.3, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000005231.3,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSBTAP00000005231.3}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000005231.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; BC120394; AAI20395.1; -; mRNA.
DR RefSeq; NP_001069551.1; NM_001076083.1.
DR STRING; 9913.ENSBTAP00000072357; -.
DR PaxDb; 9913-ENSBTAP00000005231; -.
DR Ensembl; ENSBTAT00000005231.4; ENSBTAP00000005231.3; ENSBTAG00000004009.4.
DR Ensembl; ENSBTAT00000076692.1; ENSBTAP00000072357.1; ENSBTAG00000004009.4.
DR GeneID; 537070; -.
DR KEGG; bta:537070; -.
DR CTD; 5372; -.
DR VEuPathDB; HostDB:ENSBTAG00000004009; -.
DR VGNC; VGNC:33072; PMM1.
DR eggNOG; KOG3189; Eukaryota.
DR GeneTree; ENSGT00390000002918; -.
DR HOGENOM; CLU_065642_0_1_1; -.
DR OMA; FCLHYMA; -.
DR OrthoDB; 167037at2759; -.
DR TreeFam; TF300874; -.
DR Reactome; R-BTA-446205; Synthesis of GDP-mannose.
DR UniPathway; UPA00126; UER00424.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000004009; Expressed in retina and 104 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004615; F:phosphomannomutase activity; IBA:GO_Central.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006013; P:mannose metabolic process; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
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:SF1; PHOSPHOMANNOMUTASE 1; 1.
DR Pfam; PF03332; PMM; 1.
DR SFLD; SFLDF00445; alpha-phosphomannomutase; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 2: Evidence at transcript level;
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|PIRSR:PIRSR605002-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136}.
FT ACT_SITE 19
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-1"
FT ACT_SITE 21
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-1"
FT BINDING 19
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT BINDING 21
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT BINDING 235
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
SQ SEQUENCE 262 AA; 29862 MW; 4F49D4ECA393BA2A CRC64;
MAVTAEGARR KERVLCLFDV DGTLTPARQK IDPEVAAFLQ KLRSRVQIGV VGGSDYSKIA
EQLGEGDEVI EKFDYVFAEN GTVQYKHGRL LSKQTIQNHL GEELLQDLIN FCLRYMALLR
LPKKRGTFIE FRNGMLNISP IGRSCTLEER IEFSELDKKE KIREKFVEAL KTEFAGKGLR
FSRGGMISFD VFPEGWDKRY CLDSLDQDCF DTIHFFGNET SPGGNDFEIY TDPRTVGHSV
VSPQDTVQRC RELFFPETAH KA
//
