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Database: UniProt
Entry: A0A1R3HTH6_9ROSI
LinkDB: A0A1R3HTH6_9ROSI
Original site: A0A1R3HTH6_9ROSI 
ID   A0A1R3HTH6_9ROSI        Unreviewed;      1079 AA.
AC   A0A1R3HTH6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Phosphoglycerate kinase {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
DE            EC=2.7.2.3 {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
GN   ORFNames=COLO4_26973 {ECO:0000313|EMBL:OMO73622.1};
OS   Corchorus olitorius.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX   NCBI_TaxID=93759 {ECO:0000313|EMBL:OMO73622.1, ECO:0000313|Proteomes:UP000187203};
RN   [1] {ECO:0000313|Proteomes:UP000187203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. O-4 {ECO:0000313|Proteomes:UP000187203};
RA   Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA   Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA   Rashid M.M., Khan S.A., Rahman M.S., Alam M., Yahiya A.S., Khan M.S.,
RA   Azam M.S., Haque T., Lashkar M.Z.H., Akhand A.I., Morshed G., Roy S.,
RA   Uddin K.S., Rabeya T., Hossain A.S., Chowdhury A., Snigdha A.R.,
RA   Mortoza M.S., Matin S.A., Hoque S.M.E., Islam M.K., Roy D.K., Haider R.,
RA   Moosa M.M., Elias S.M., Hasan A.M., Jahan S., Shafiuddin M., Mahmood N.,
RA   Shommy N.S.;
RT   "Corchorus olitorius genome sequencing.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBUNIT: Monomer. {ECO:0000256|RuleBase:RU000696}.
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:OMO73622.1}.
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DR   EMBL; AWUE01019409; OMO73622.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R3HTH6; -.
DR   OrthoDB; 446644at2759; -.
DR   Proteomes; UP000187203; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008176; F:tRNA (guanine(46)-N7)-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 2.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
DR   InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR   InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb.
DR   PANTHER; PTHR11406; PHOSPHOGLYCERATE KINASE; 1.
DR   PANTHER; PTHR11406:SF32; PHOSPHOGLYCERATE KINASE; 1.
DR   Pfam; PF02390; Methyltransf_4; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS51625; SAM_MT_TRMB; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000532};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187203};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000532}.
FT   REGION          697..721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1002..1029
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        698..721
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1079 AA;  120998 MW;  C8EF192D92B12758 CRC64;
     MKFLRHGSWK YPINNVQSSL QGGLEVVTHV ESSHKEQTCL YDGVELEALP HIQTLKNFPK
     EELFANVVMV RFDSNILLGE KLDWSSQSAS KALYTIKYLH KSGAKVILVS SWKRKKNSEL
     LAAEAVADIL SSVLQHKVVA LRCISCDMPV KGEDLQKADI FLLENLSDYK EEVSNCSKFA
     ELLSSEVDIF VNDSFSQSHK VLASTVGVAR FCYASMAGFL FEESLHQLKK TAKTNKKPYI
     AIIGGGNLNN KAAAIEFLAS RCDALVFVGL MSFQIMHALG HSVPTNLLER EAHKTALDIV
     QFAHEKHVLI SYPEDFWCVN QHLPKQMGVF PAHGVLDGWL PVDLGPKSLD EINSLVTNSK
     RVIWIGPVKF KSYSPYTGGT SKLAQMLYKQ SQCDCEVTIV GSMAHEIAKN ESGSVSSFNM
     LENASAVWEF LKGQKLPGVV ALDRAYPFEI DWNVAYCDPS RPLVVDIGSG NGLFIMGMAR
     KRKDLNFLGL EINGKLVRRC LDSVHQSGIT NGYFIETNAT STFRSIVSSY PGELVLASIQ
     CPNPDFNKPE HRWRMLQRSL IEAVADLLAS KGKVFLQSDV EEVAMRMKEL FLKYGKGKLC
     LSHDHHNVRA NGNTWLEENP YGIRSDWEQH VLDRGAPILF IEKLSVIVAM IDSFLEVQSS
     TVMKIALPDN IWKQLQHTLM IAGHAKYVRR EENTNFPEDL TESTFPNETQ EELSQSTALP
     HPTSDVDDDI FAEARKSGLD IRYSIVSDGF PLGFDRSLNH DQFFEGVLHV MSAHIDELVA
     NTFKQSPPPT CLIADTFYVW SSMISNKYNL VNVSFWTEPA LVFTLYYHLD LLRANGHFAC
     TENRKDIIDY IPGVRAIEPK DMMSYLQASD ISTVVHRIIF KAFEDVKKAD FIICNTVEEL
     EHETISALQE KQPTYAIGPI FPTGFTKSVV ATSLWSESDC TQWLDTKPHG SVLYVSFGSY
     AHVSKIEIAE VANGLLLSGK QNKWDKVAEK IHHVIGGKSN DDDELRKNIK EVKRKLENAL
     SAVGSSEKNF NQFIRDMEMK SKKKRASAMC CEVDNVVQSV QTVIYLFLAA IYNKLPSSS
//
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