ID A0A1R3GG40_COCAP Unreviewed; 691 AA.
AC A0A1R3GG40;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013068, ECO:0000256|RuleBase:RU003994};
DE EC=4.1.2.13 {ECO:0000256|ARBA:ARBA00013068, ECO:0000256|RuleBase:RU003994};
GN ORFNames=CCACVL1_26076 {ECO:0000313|EMBL:OMO57029.1};
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:OMO57029.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO57029.1, 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:OMO57029.1};
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=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
CC Evidence={ECO:0000256|ARBA:ARBA00000441,
CC ECO:0000256|RuleBase:RU003994};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC {ECO:0000256|ARBA:ARBA00004714}.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000256|ARBA:ARBA00010387, ECO:0000256|RuleBase:RU003994}.
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:OMO57029.1}.
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DR EMBL; AWWV01014432; OMO57029.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3GG40; -.
DR STRING; 210143.A0A1R3GG40; -.
DR EnsemblPlants; OMO57029; OMO57029; CCACVL1_26076.
DR Gramene; OMO57029; OMO57029; CCACVL1_26076.
DR OrthoDB; 3595068at2759; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000188268; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00948; FBP_aldolase_I_a; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR029768; Aldolase_I_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR021788; CPP1-like.
DR InterPro; IPR000741; FBA_I.
DR NCBIfam; NF033379; FrucBisAld_I; 1.
DR PANTHER; PTHR11627; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR11627:SF58; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR Pfam; PF11833; CPP1-like; 1.
DR Pfam; PF00274; Glycolytic; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|RuleBase:RU003994};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003994};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 181..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 691 AA; 75601 MW; 94517415A98ABCCB CRC64;
MNISGLTGSP SKCCLRLPDH SRRLVCRHGS AFLGAGKPKE KFGLLSLERS SRAISVRKWK
TQNTHLIKCA MDASYGDMAS ESSGSAVFPR INVKDPYKRL GISREASEDE ILAARNFLIS
RYGGHKPSVD AIEAAHDKII MQKFYERKNP KIDIKKKVRE VKQSRVVQAV TSRFQTPATK
VIVKTSIAFI VLGVLTVLFP TEEGPTLQVA ISLIATFYFI NDRLKSKIRA LLYGAGAFLF
SWLVGTFLMV SVIPPIPILK GPRTFEVLTS LITYVLLKEA CGEREIRAIY FQNSKMASAS
LLKTSPVVDK SEWVRGQPLR QPSVSVVRCN RVATSGLTVR ASSYADELVK TAKTIASPGR
GILAMDESNA TCGKRLASIG LENTEANRQA YRTLLVSAPG LGQYISGAIL FEETLYQSTV
DGKKMVDVLT EQNIVPGIKV DKGLVPLAGS NNESWCQGLD GLAPRSAAYY QQGARFAKWR
TVVSIPNGPS ELAVKEAAWG LARYAAISQD NGLVPIVEPE ILLDGEHGID RTFEVAKKVW
AEVFFYLAQN NVLFEGILLK PSMVTPGAEC KDRATPQQVA DYTLSLLRQR IPPAVPGIMF
LSGGQSEVEA TLNLNAMNQA PNPWHVSFSY ARALQNTCLK TWGGLPENVK AAQDALLVRA
KANSLAQLGK YTGEGESEEA KQGMFVKGYV Y
//
