ID A0A0V1NNL1_9BILA Unreviewed; 933 AA.
AC A0A0V1NNL1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=phosphoglycerate mutase (2,3-diphosphoglycerate-independent) {ECO:0000256|ARBA:ARBA00012026};
DE EC=5.4.2.12 {ECO:0000256|ARBA:ARBA00012026};
GN Name=MVK {ECO:0000313|EMBL:KRZ85537.1};
GN ORFNames=T08_14366 {ECO:0000313|EMBL:KRZ85537.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ85537.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ85537.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ85537.1};
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:KRZ85537.1}.
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DR EMBL; JYDM01000140; KRZ85537.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1NNL1; -.
DR STRING; 92180.A0A0V1NNL1; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000054924; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProt.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:UniProt.
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; IPR006204; GHMP_kinase_N_dom.
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; PF00288; GHMP_kinases_N; 1.
DR Pfam; PF06415; iPGM_N; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR PRINTS; PR00959; MEVGALKINASE.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924}.
FT DOMAIN 161..244
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 315..380
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
FT DOMAIN 429..919
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
FT DOMAIN 505..718
FT /note="BPG-independent PGAM N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06415"
SQ SEQUENCE 933 AA; 102642 MW; EFC11BCE17DAC43F CRC64;
MPACESGEGG WEGVFRGEGR LAMMITMTEP SNSINISAPG KIILFGEHAV IYGRTAVAGC
IDLRTYVNLF TSADGRIYLS LPDLGVERTW LMKDVRKAVD KLYEGKSDDN APPCLELVVP
IARQICGTSE DQCGVQQLAS LAFLYLLIGV ARKRKDLLAV KVTVRFNLPS CVGLGSSGAY
CVCIAAALLQ VAEIIPSPTV TAANNASTWS PQHLETIRLW ASAAESLIHG RASGLDATIC
TYGGVASYRH GCKIEQLEKY CIFPEVIDGI FNAIDAISRD AIKILGQPQH SKNRKTCSED
EHYSLQEWSM ELYSDVNELC RINNQLLIAL GVGHPKIDQI CTTLARYGIH PKMTGAGGGG
SLFAFLKPNT SQTVIDMITS EVHKLGYDLW QPKLGGSGVV LHSSIPEEFR LTNEKFYYYT
MSCAKVTQPV CLVVIDGWGM CGSANGNAIC NAKTPVMTRL FGENSTQLEA HGLHVGLPEG
LMGNSEVGHL NIGAGRVVYQ DIVRINMAVT SGKIKENATL VNACKNASNK NGRLHLLGLV
SDGGVHSHIK HMFGLLEAAK YHKVPKCFIQ FFSDGRDTSP TSGVRFVEEV FNFTKSIQYG
QLATVVGRYY AMDRDKRWER NQIAYEGLVA GRGEKATEDT LIEVIKKSYD NNVTDEFLKP
IIVNDEGRIK DDDTLIFFDY RADRMRQIVE AFGIKRNFET DVAHPKNLHI SCMTQYNKDF
TFPLLFPPES HKNVLAEWLA ANSIPQFHCA ETEKYAHVTF FFNGGREAPF DHEDRLMIPS
PKVATYDLKP EMSCMEVGSK MAEIIRTKNY PFVMCNFAPP DMVGHTGIYE AAVKACEATD
CAIGLVEKAC QEAGYVLMIT ADHGNAEQMF DPKGGKHTAH TCNRVPFIST GKRRLMAKLP
DREPALCDVA PTVLDQMGLA IPSEMGGKSL LQN
//
