ID A0A090L8W3_STRRB Unreviewed; 1653 AA.
AC A0A090L8W3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=SRAE_2000084200 {ECO:0000313|EMBL:CEF66172.1,
GN ECO:0000313|WBParaSite:SRAE_2000084200.1,
GN ECO:0000313|WormBase:SRAE_2000084200};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF66172.1};
RN [1] {ECO:0000313|EMBL:CEF66172.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_2000084200.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF66172.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_2000084200.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) 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; LN609529; CEF66172.1; -; Genomic_DNA.
DR STRING; 34506.A0A090L8W3; -.
DR EnsemblMetazoa; SRAE_2000084200.1; SRAE_2000084200.1; WBGene00261042.
DR WBParaSite; SRAE_2000084200.1; SRAE_2000084200.1; WBGene00261042.
DR WormBase; SRAE_2000084200; SRP11299; WBGene00261042; -.
DR eggNOG; KOG0401; Eukaryota.
DR OrthoDB; 167037at2759; -.
DR UniPathway; UPA00126; UER00424.
DR Proteomes; UP000035682; Chromosome X.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02585; HAD_PMM; 1.
DR Gene3D; 1.25.40.180; -; 1.
DR Gene3D; 3.30.1240.20; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR003890; MIF4G-like_typ-3.
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; PF02854; MIF4G; 1.
DR Pfam; PF03332; PMM; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU361118};
KW Hydrolase {ECO:0000313|EMBL:CEF66172.1};
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:UP000035682}.
FT DOMAIN 543..784
FT /note="MIF4G"
FT /evidence="ECO:0000259|SMART:SM00543"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 640..672
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 23..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1613
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT BINDING 1625
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT BINDING 1627
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT BINDING 1630
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
SQ SEQUENCE 1653 AA; 188108 MW; C8DA26FD8A00E034 CRC64;
MSTHLSNPHN KGGNKNRGSR KNTYRGPHVN SGNYINHTEN NYTSNSQHIT QPEVQFATPQ
LLNVSYSAPE HHPQPQMQHT HHNVAGQVDQ PTNLIHTQVT TMPYFNGHQA PMGYVQPTAP
IPLPVFHPNA ISYSQPGQVP QNYPPAIESY QVPQPVNYRP IPAPVPGSTE FELVECKKPA
VIQKKEKRIL SVCDPETKKS IFDEGASNLN KDISSKESTP SEVTLHKSAS GSSVKQHLVI
EKAPSIRSRQ NSERVSELGG NNNEGSNWIK EEFKRQIAER AVGSSTEAAL GDKIKPEDET
VKDERDPINN IISQAEILAN TISESIEKLE LEAPSKEVID GQKEEEVKTE SKNETDTSGN
LITSSSTLVK GTSKDQVQKK LSFASEQPKI EKKADKETYL EIEADMKRSM EDPKFDIENC
VYPKNFIRTY RLAVSLFKIA SNPVSDEIKA LLYYDKSSIS TSMKGRRNDN QFQPPWSKTV
NDQGRKSYGG RNSHGHSSDR RKNRNNAVAR PSIERSRANV QLHRSENAWK PSACSDDINS
KLLKEVRGIL NKITPTNFEA LMTEFLQFRL FEKKEILQDV IDLIFAKAVE EPRFCSIYSD
LYNAQVNDEK KQTSSVKSSF GTALIQKCQV TFEKKDFPFS KEMEQINEEL KSETDEEKIK
EKTDRLAELV EKEKRFTFGT IRFIAHLYRH DLLVTKIISY CVTYLLNMFQ NENNEKALEQ
AVLLFETVGK HWSGLPRNSE NNSDIGMSLQ HFKKYLPNNE SNPYNLSKRM QFMIENLIET
SENNWVAKNS RMRDGPKKID EVHEEIKNEE MQNAYLRDQY SKEKDNESSK RKPYSGTNSV
DKRYNLSKNS SINRKNTDLR DSGHYTLKTQ AKSFADGCNP KDTKTINEKS GTIPRSKKSD
GGRKDGNSSK RQASPQWSRP STNSRKSTKA VECFDDDFYN DQTPEVTIVD VKYNKDELNK
QLKQLANDHG QPDKIAELKD MIERYLNEEN CCEVVETIML FVFYDINKVR STIERATIGR
LIGCLLSGPK NAEVLHGLVS LCEHFDDFGV TSDCPRAWIY FGELLANAII YDTSTNVSSE
KLTLDKLDRI FSAAEPKETK DEFLFAFLKS TITEENLLEP IEDNEKRDEF IKSLVISINK
MKLTDTGIIS EKMEEKLKNV SSKRDNKNLL EVIKGYETLP FLSSEGTNSL LQFGKAKKVE
DFGEPTINVD LELNKKNAEI PVKVLPKGIY TYSDTQRDFN SNFKLPDINN PIDISGFMKS
KNNYINGLYL PMPFGMEPVN VQFFRENEQE NAIEGAFSTE GKIIKAKEKA KVICNKGPTK
ECDEALEEYY ILMSDNVNEK DAPLFEKLVK LTDSIGSAGY RDNKKKGLGV LLGLPGMEDP
VYWKARFDNF NDNSIFLNAN MPNSCNATIG NVFIRILIMI ESRQTISNEN LQFFKELSKN
QNLGIVGGSD FGKICEQMGL SEEDLCSTFS YVFAENGLDG KINGKQIQKQ SILKFLGDSK
YQILINYIFK LFSEIDIPKK RGNFVELRNG MINISPIGRS CTQEERIEFF LYDQQHNVRR
EIVEKLKEKF TEYELDFVIG GQISIDIFPL GWDKRYCLKY IEGEFEKIYF FGDKTMPGGN
DYALFIDNRT IGHTVSGPDD TVKQVKDIIN NLK
//
