ID A0A0V1CB51_TRIBR Unreviewed; 568 AA.
AC A0A0V1CB51;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 03-MAY-2023, entry version 27.
DE RecName: Full=Phosphoglycerate kinase {ECO:0000256|RuleBase:RU000532};
DE EC=2.7.2.3 {ECO:0000256|RuleBase:RU000532};
GN Name=pgk-1 {ECO:0000313|EMBL:KRY46312.1};
GN ORFNames=T03_4329 {ECO:0000313|EMBL:KRY46312.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY46312.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY46312.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY46312.1};
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 -!- FUNCTION: May be involved in cell cycle regulation.
CC {ECO:0000256|ARBA:ARBA00002646}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC Evidence={ECO:0000256|RuleBase:RU000532};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5. {ECO:0000256|ARBA:ARBA00004838,
CC ECO:0000256|RuleBase:RU000532}.
CC -!- SUBUNIT: Interacts with UHRF2/NIRF. {ECO:0000256|ARBA:ARBA00011097}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245,
CC ECO:0000256|RuleBase:RU000696}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000256|ARBA:ARBA00008982, ECO:0000256|RuleBase:RU000532}.
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:KRY46312.1}.
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DR EMBL; JYDI01000295; KRY46312.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1CB51; -.
DR STRING; 45882.A0A0V1CB51; -.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
DR Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 3.
DR HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR InterPro; IPR029169; PCNP.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR PANTHER; PTHR11406; PHOSPHOGLYCERATE KINASE; 1.
DR PANTHER; PTHR11406:SF0; PHOSPHOGLYCERATE KINASE; 1.
DR Pfam; PF15473; PCNP; 1.
DR Pfam; PF00162; PGK; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000532};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000532};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT REGION 526..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 62026 MW; 18B9DCAC875940E3 CRC64;
MHKGSIAYKY KVYFDDLLTI MALNKLAIDN VDLEGKRVII RVDFNVPMKD GKITNPQRIV
ESLPTIKYAL EKGARSLILM SHLGRPEGQK NMKYSLRPVA EELSKLLNKN VQFLPDCVGE
EVEAACKACS PGSVILLENL RFHIEEEGKG VNEAGEKIKA SKEQIEKFQK SLTSLADVYV
NDAFGTAHRA HSSMVGVQLS VRCSGFLLKK ELQFFAKALE NPERPFLAIL GGAKVADKIQ
LIKNLLDKVN EMIIGGGMAF TFLKQLHGMN IGNSLFDEEG AKIVKELMEK AKKNGVKIHL
PVDIVTGDKF DEKAAVGSAT VQTGIPDGWM GLDVGPVTRK LFSEAIDRAK TIVWNGPPGV
FEWDNFAAGT KAMMDSVVKA TEKGATTIIG GGDTATCCAK FKTEHKVSHV STGGGASLEL
LEGKILPGVA ALSGLNIVGG KRKIEEAQQS TSASTEVSHK ALSSKGKIKI KLKIHKTTES
DNASEQQKEE TPKAPTLLKP LLNVFDDDSD GKEAEEMPAE CRRRMRNFGR DTPTSSGPNS
FSKGKHGFVD ARKVAERRLQ MMTREIDD
//
