ID A0A1R3GIZ6_COCAP Unreviewed; 1437 AA.
AC A0A1R3GIZ6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Pyruvate kinase {ECO:0000256|RuleBase:RU000504};
DE EC=2.7.1.40 {ECO:0000256|RuleBase:RU000504};
GN ORFNames=CCACVL1_25611 {ECO:0000313|EMBL:OMO58041.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO58041.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO58041.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO58041.1};
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.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC EC=2.7.1.40; Evidence={ECO:0000256|ARBA:ARBA00001174,
CC ECO:0000256|RuleBase:RU000504};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5. {ECO:0000256|ARBA:ARBA00004997,
CC ECO:0000256|RuleBase:RU000504}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC {ECO:0000256|ARBA:ARBA00008663, ECO:0000256|RuleBase:RU000504}.
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:OMO58041.1}.
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DR EMBL; AWWV01014261; OMO58041.1; -; Genomic_DNA.
DR STRING; 210143.A0A1R3GIZ6; -.
DR EnsemblPlants; OMO58041; OMO58041; CCACVL1_25611.
DR Gramene; OMO58041; OMO58041; CCACVL1_25611.
DR OrthoDB; 5483908at2759; -.
DR UniPathway; UPA00109; UER00188.
DR Proteomes; UP000188268; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR GO; GO:0004743; F:pyruvate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00288; Pyruvate_Kinase; 1.
DR Gene3D; 2.70.130.10; Mannose-6-phosphate receptor binding domain; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 2.40.33.10; PK beta-barrel domain-like; 1.
DR Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 1.
DR InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR InterPro; IPR044865; MRH_dom.
DR InterPro; IPR036607; PRKCSH.
DR InterPro; IPR028146; PRKCSH_N.
DR InterPro; IPR001697; Pyr_Knase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR InterPro; IPR018209; Pyrv_Knase_AS.
DR InterPro; IPR015793; Pyrv_Knase_brl.
DR InterPro; IPR015795; Pyrv_Knase_C.
DR InterPro; IPR036918; Pyrv_Knase_C_sf.
DR InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR NCBIfam; TIGR01064; pyruv_kin; 1.
DR PANTHER; PTHR11817; PYRUVATE KINASE; 1.
DR PANTHER; PTHR11817:SF34; PYRUVATE KINASE; 1.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR Pfam; PF12999; PRKCSH-like; 1.
DR Pfam; PF13015; PRKCSH_1; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF50911; Mannose 6-phosphate receptor domain; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR SUPFAM; SSF52935; PK C-terminal domain-like; 1.
DR PROSITE; PS51914; MRH; 1.
DR PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU000504};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000504};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU000504};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:OMO58041.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000504}.
FT DOMAIN 760..855
FT /note="MRH"
FT /evidence="ECO:0000259|PROSITE:PS51914"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1437 AA; 157507 MW; 073EBABE8B489DA6 CRC64;
MESSSATVNE PRSASPPPNS QNPTPELHTD PNSQIPSSSQ PTQNTTTASV NARKTLPAAI
NKATKGASSS SATGSAAGYG PARVKAKASA CPAVMATATV TARPASQDHC PNQKQKVKGK
QKQPWKHPGV SFADSDGRLY GQMGIGRTSP LSKSKGTKFM VGKKFVPSNS IGASGSKGKK
NQPPAAPNYK PSKKRMAGLG ICPETGRFIT SLGEPSQKSA CVGNIQKKAR TNADSLNDGA
SSRTDMGPKE GCDETSEWTV APLVRDSFSM IGSAVGGTTS AFYGFNHVMP IVRRWVKGPM
WVHFLIGAPP VIVFSSACAG LTGGAVPALA QLASSSYHAA FSSSSLPPSS PEDKMHNKSR
TSSTFEQELH CGSGTILVYN LIKNEDYFKG EIINCKNGSK KFTRTQLNDD FCDCPDGTDE
PGTSACPLGK FYCRNAGHSP SLLFSSRVND GICDCCDGSD EYDGKVKCPN TCWEAGNVAR
DNLKKKIEMY HEGVALRKQE IQKAKQAIAR DNVELLGLKN EKEVLQKLVK QLEEQIQKLE
QKERLEKEEK MKDAFTENVE NEKSGPEENV VSQKEALKIS HDEKMGISGK TLSDQKEKES
TEGLSREELG RLVASRWTGK KTEDQVGEIN TGKSDKEESA DDDHQEKGRN DAGAEDSVSG
NTGHSSVNFN MKLEYHEKST GTEILSHQSW LDKIQEAGQN LLQSVNLFSA HVANLDLYQV
RNEYKNYTAR LSDIEPRILS LTEKFKYDFG IEKEFYLFYD SCFESKQDKY VYKVCPFKRA
TQEEGSSETR LGNWEKFGNS YRMMLFTNGE RCWNGPDRSL KVKLRCGLKT ELTGVDEPSR
CEYVALLYTP ALCLEQKLKL YFIPKSGPET RSRLQLRQIN QTSFCLTSSN CYNFFQLFIS
FLRLRTRNKI FVVPSRLLGV RISRKQLNGE SMSGVIRAME NVLSKAEAMV RPKTKIVCTL
GPASRSVEMI ERLLKAGMNV ARFNFSHGSH AYHQETLDNL RTAMNNTGIL CAVMLDTKGP
EIRTGFLKDE KPIQITQGKN ITITTDYSIK GDENLISMSY KKLAEDLKPG SVILCSDGTI
TFTVLDCDKE AGLVHCRCEN SAVLGERKNV NLPGVVVDLP TLKEKDKEDI LQWGVPNKID
MIALSFVRKG SDLVEVRKLL GEHAKNILLM SKVENQEGVA NFDDILANSD AFMVARGDLG
MEIPIEKIFL AQKLMIRKAN ILGKPVVTAT QMLESMIKSP RPTRAEATDV ANAVLDGTDC
VMLSGETAAG AYPDIAVQTM ASICVEAEKF INYGDLFKRI METAPMPMSP LESLASSAVR
TANCIKAALI LVLTKGGVTA KLVSKYRPSM PILSLVMPEI ATDSLEWSCS DEAPARHCLI
YRGLVPVLSS GSAKASYDES TEESIKFALE YAKANGLCRE GDSIVALHPS VIKILTV
//
