ID A0A0V1NVK4_9BILA Unreviewed; 667 AA.
AC A0A0V1NVK4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN Name=gpa-12 {ECO:0000313|EMBL:KRZ87996.1};
GN ORFNames=T08_5796 {ECO:0000313|EMBL:KRZ87996.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ87996.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ87996.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ87996.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-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}.
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:KRZ87996.1}.
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DR EMBL; JYDM01000091; KRZ87996.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1NVK4; -.
DR UniPathway; UPA00126; UER00424.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IEA:InterPro.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:InterPro.
DR CDD; cd00066; G-alpha; 1.
DR CDD; cd02585; HAD_PMM; 1.
DR Gene3D; 3.30.1240.20; -; 1.
DR Gene3D; 1.10.400.10; GI Alpha 1, domain 2-like; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR000469; Gprotein_alpha_12/13.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005002; PMM.
DR InterPro; IPR043169; PMM_cap.
DR NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR PANTHER; PTHR10218; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1.
DR PANTHER; PTHR10218:SF362; GUANINE NUCLEOTIDE-BINDING PROTEIN SUBUNIT ALPHA HOMOLOG; 1.
DR Pfam; PF00503; G-alpha; 1.
DR Pfam; PF03332; PMM; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00440; GPROTEINA12.
DR SFLD; SFLDF00445; alpha-phosphomannomutase; 1.
DR SFLD; SFLDG01143; C2.B.3:_Phosphomannomutase_Lik; 1.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF47895; Transducin (alpha subunit), insertion domain; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|PIRSR:PIRSR605002-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR605002-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT ACT_SITE 428
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-1"
FT ACT_SITE 430
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-1"
FT BINDING 428
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT BINDING 430
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT BINDING 630
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT BINDING 642
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT BINDING 644
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
FT BINDING 647
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR605002-3"
SQ SEQUENCE 667 AA; 78128 MW; 3D881477E41F3960 CRC64;
MCSLSNLLCD CTWPDSNKLQ SKRIDVELKK QKKKLRREIS VLLLGTGESG KSTFLKQMVI
IHGRGEFTVD EIYEYKLLIF ANILNGMRIL IAARKFFDDI VWQYPEQSAN LSQQFAKLCP
AEFSAQRLNV AETFTKCAPL VTELWNDSAI RETFERRREF QLPDSCKYFF ENIARISQAS
YAPSNRDILL CRKATRAITE HVFDIQNVPF RFIDVGGQRS QRQKWFECFE GVTSILFLVA
SNEYDQVLLE DRRKNRLLES REVYDTIVNN RFFSDISFIL FFNKTDLLSE KITRSDIRDN
FENFQGNPHS LHDVQFFFLG LFDSVRKNKA QPFFYHFTTA IDTDNIRRVF KDCKEIILDR
NLKTLMMHGT LDTEYNKKVV CIMPLSRLDF IRLLEILSIS AFWSTCSSCG RLKVFSVISR
LKRICLFDVD GTLTRPRQKI DNDFLEYLRS LSKKIPLAVV GGSDIDKVLE QLDLNLKDAC
DLFEYVFAEN GLFVAKKNQQ FPTATIQEVI GEEKLQEFIN YCLHYLSEVK LPVKRGNFIE
FRKGMLNVSP IGRSCSQNER NEFVEYDEKH QIREKFIEEL RKRFPVEKYG LHFSIGGQIS
IDVFPVGWDK RYCLQFLEKD DFREIYFFGD RTFPGGNDYE IFEDPRTIGH RVTSPKDTER
ELKSLFG
//
