ID A0A0V0WLT1_9BILA Unreviewed; 774 AA.
AC A0A0V0WLT1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=phosphoglycerate mutase (2,3-diphosphoglycerate-independent) {ECO:0000256|ARBA:ARBA00012026};
DE EC=5.4.2.12 {ECO:0000256|ARBA:ARBA00012026};
DE Flags: Fragment;
GN Name=MVK {ECO:0000313|EMBL:KRX76703.1};
GN ORFNames=T06_3928 {ECO:0000313|EMBL:KRX76703.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX76703.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX76703.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX76703.1};
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=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|ARBA:ARBA00004798}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. {ECO:0000256|ARBA:ARBA00008819}.
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:KRX76703.1}.
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DR EMBL; JYDK01000095; KRX76703.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0WLT1; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0006007; P:glucose catabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd16010; iPGM; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 3.40.1450.10; BPG-independent phosphoglycerate mutase, domain B; 1.
DR Gene3D; 3.30.70.890; GHMP kinase, C-terminal domain; 1.
DR HAMAP; MF_01038; GpmI; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR011258; BPG-indep_PGM_N.
DR InterPro; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR036646; PGAM_B_sf.
DR InterPro; IPR005995; Pgm_bpd_ind.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR01307; pgm_bpd_ind; 1.
DR PANTHER; PTHR31637; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR31637:SF0; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF06415; iPGM_N; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR SUPFAM; SSF64158; 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673}.
FT DOMAIN 156..221
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
FT DOMAIN 270..760
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
FT DOMAIN 346..559
FT /note="BPG-independent PGAM N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06415"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX76703.1"
SQ SEQUENCE 774 AA; 86003 MW; 16B14D591947E242 CRC64;
LAMMITMTEP SNSINISAPG KIILFGEHAV IYGRTAVAGC IDLRTYVNLF TSADGRIYLS
LPDLGVERTW LMKDVRKAVD KLYGGVASYR HGCKIEQLEK YCIFPEVIDG IFNAIDAISR
DAIKILGQPQ HSKNRKTCSE DEHYSLQEWS MELYSDVNEL CRINNQLLIA LGVGHPKIDQ
ICTTLARYGI HPKMTGAGGG GSLFAFLKPN TSQTVIDMIT SEVHKLGYDL WQPKLGGSGV
VLHSSIPEEF RLTNEKFYYY TMSCAKVTQP VCLVVIDGWG MCSSANGNAI CNAKTPVMTR
LFGENSTQLE AHGLHVGLPE GLMGNSEVGH LNIGAGRVVY QDIVRINMAV TSGKIKENAT
LVNACKNASN KNGRLHLLGL VSDGGVHSHI KHMFGLLEAA KYHKVPKCFI QFFSDGRDTS
PTSGVRFVEE VFNFTKSIQY GQLATVVGRY YAMDRDKRWE RNQIAYEGLV AGRGEKATED
TLIEMIKKSY DNNVTDEFLK PIIVNDEGRI KDDDTLIFFD YRADRMRQIV EAFGIKRNFE
TDVAHPKNLH ISCMTQYNKD FTFPLLFPPE SHKNVLAEWL AANSIPQFHC AETEKYAHVT
FFFNGGREAP FDHEDRLMIP SPKVATYDLK PEMSCMEVGS KMAEIIRTKN YPFVMCNFAP
PDMVGHTGIY EAAVKACEAT DCAIGLVEKA CQEAGYVLMI TADHGNAEQM FDPKGGKHTA
HTCNRVPFIS TGKRRLMAKL PDREPALCDV APTVLDQMGL AIPSEMGGKS LLQN
//
