ID A0A072TDV2_MEDTR Unreviewed; 1918 AA.
AC A0A072TDV2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Phosphoribulokinase, chloroplastic {ECO:0000256|ARBA:ARBA00017837};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.7.1.19 {ECO:0000256|ARBA:ARBA00012042};
DE EC=3.1.3.11 {ECO:0000256|ARBA:ARBA00013093};
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase {ECO:0000256|ARBA:ARBA00032973};
GN ORFNames=MTR_0776s0010 {ECO:0000313|EMBL:KEH15587.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880 {ECO:0000313|EMBL:KEH15587.1, ECO:0000313|Proteomes:UP000002051};
RN [1] {ECO:0000313|EMBL:KEH15587.1, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:KEH15587.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:KEH15587,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [2] {ECO:0000313|EMBL:KEH15587.1, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=A17 {ECO:0000313|EMBL:KEH15587.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:KEH15587,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [3] {ECO:0000313|EnsemblPlants:KEH15587}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:KEH15587};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-
CC bisphosphate + H(+); Xref=Rhea:RHEA:19365, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57870, ChEBI:CHEBI:58121,
CC ChEBI:CHEBI:456216; EC=2.7.1.19;
CC Evidence={ECO:0000256|ARBA:ARBA00001430};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001027};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-
CC phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11;
CC Evidence={ECO:0000256|ARBA:ARBA00001273};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the FBPase class 1 family.
CC {ECO:0000256|ARBA:ARBA00010941}.
CC -!- SIMILARITY: Belongs to the phosphoribulokinase family.
CC {ECO:0000256|ARBA:ARBA00009719}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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DR EMBL; KL403500; KEH15587.1; -; Genomic_DNA.
DR RefSeq; XP_013441562.1; XM_013586108.1.
DR STRING; 3880.A0A072TDV2; -.
DR EnsemblPlants; KEH15587; KEH15587; MTR_0776s0010.
DR Gramene; KEH15587; KEH15587; MTR_0776s0010.
DR HOGENOM; CLU_235436_0_0_1; -.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000002051; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008974; F:phosphoribulokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004802; F:transketolase activity; IBA:GO_Central.
DR GO; GO:0006098; P:pentose-phosphate shunt; IBA:GO_Central.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd00009; AAA; 1.
DR CDD; cd00354; FBPase; 1.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.190.80; -; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_01855; FBPase_class1; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041627; AAA_lid_6.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR000470; CbxX/CfqX_mono.
DR InterPro; IPR000641; CbxX/CfxQ.
DR InterPro; IPR044015; FBPase_C_dom.
DR InterPro; IPR000146; FBPase_class-1.
DR InterPro; IPR033391; FBPase_N.
DR InterPro; IPR028343; FBPtase.
DR InterPro; IPR020548; Fructose_bisphosphatase_AS.
DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR023198; PGP-like_dom2.
DR InterPro; IPR006082; PRK.
DR InterPro; IPR006083; PRK/URK.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR005478; Transketolase_bac-like.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR049557; Transketolase_CS.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR NCBIfam; TIGR02880; cbbX_cfxQ; 1.
DR NCBIfam; TIGR01549; HAD-SF-IA-v1; 1.
DR NCBIfam; TIGR00232; tktlase_bact; 1.
DR PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17866; AAA_lid_6; 1.
DR Pfam; PF00316; FBPase; 1.
DR Pfam; PF18913; FBPase_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR Pfam; PF13419; HAD_2; 1.
DR Pfam; PF00485; PRK; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR PIRSF; PIRSF500210; FBPtase; 1.
DR PIRSF; PIRSF000904; FBPtase_SBPase; 1.
DR PRINTS; PR00819; CBXCFQXSUPER.
DR PRINTS; PR00820; CBXXCFQX.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00846; Gp_dh_N; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS00124; FBPASE; 1.
DR PROSITE; PS00567; PHOSPHORIBULOKINASE; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 62..201
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 651..886
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 1279..1453
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT DOMAIN 1789..1909
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
SQ SEQUENCE 1918 AA; 210991 MW; ED16EB651F70AAD5 CRC64;
MSTETAIDLQ AIVRDAQISD VLERLDRELV GLVPVKTRIG EIAAFLVVER ARKELGMATA
APSLHMCFTG NPGTGKTTVA MRMAEILHRL GYVRKGHVVA VTRDDLVGQY IGHTAPKTKE
VLKRAMGGVL FIDEAYYLYR PENERDYGQE AIEILLQIME NQRDDLVVIL AGYKDRMDTF
FKSNPGMASR IAHHIDFPDY TDGELLDIAE LMLHDMHYRL DDGAKVALCE YIERRKAQPH
FANARSIRNA LDRARLRQAN RIFSSTEVVT REALQTIVAA DIRASRHGRT TLSKFIIEEH
RRHPAQDEQL TALINDIQTA CKYIGARVAR GALDGAIGAA GMKNVQGETQ QKLDVISNDI
MLQCCEWGGQ LAGMVSEELE HAYEIPEQFP RGRYLLLFDP LDGSSNIDVN LTVGTIFSVL
EAPPGVSNPQ LADFLQPGTA QVCGGYALFG PADMIVLTLG RGVHGFTLDP EIGAYILTHS
DLRISEETQE FAINASNMRF WEPPVRRYID ECLNGKSGPR QQDFNMRWVA SLVAEVHRIL
MRGGVFMYPK DSKDPAKPGR LRLLYEANPM AMIVEQAGGC ASTGRGRILD VAPEALHQRV
PVILGSRREV EPALMRDSIR RYSTHARCSA RLPDAFARRI SYKDGGDMST KHPIVAITGS
SGAGTTTITK AFQHIFRREA VNAAIVEGDS FHAYDRMQMR QKLKEAEEAG NDNFSHFGPE
GNLFDALEAL FENYGATGTG RCRRYLHDEA EGAEHGQPPG TFTPWADLPG GTDLLFYEGL
HGAVVTDNVD VARHADLLVG VVPIINLEWI QKLHRDQNMR GYSQEAVVDT ILRRMPDYVS
YICPQFSHTH VNFQRVPVVD TSNPFIARDI PSLDESMLVI RFANPKGIDF PYLLSMLNGS
ERRRSHKRGF AMNHPSHARY QATASQSRRR FANALRFLAI DAVEAAKSGH PGMPMGMADI
AEVLWRDHLR HNPADPSWSN RDRFILSNGH GSMLLYAALH LSGYDLPLDE LKHFRQLHAK
TPGHPEVDVT PGVETTTGPL GQGLANGVGM ALAEKLLAAR FNRPGHAIVD HRTYVFLGDG
CLMEGISHEA GSLAGTLGLG KLICFYDDNG ISIDGHVNGW FTDDTAARFS AYGWNVIGPI
DGHDAAAVDA AIRDAHACDE RPSLIICKTT IGWGSPNKAD THDVHGAPLG TDEIAATRDA
LEWHHPPFEI PADVRASWSQ RERGAALVAN WEGLFESYRT GYPDEAAEFE RRMRSELPAD
WPSIARRLLE AARDVTSPTA TRRSSQIALE VLVPELPELF GGSADLTGSN LTAVKASRTL
NGTPVVDRGA NYMSYGVREF GMIAMMNGLA LHGGFIPYGG TFLVFSDYAR NAIRMSALMN
RRVIHVLTHD SIGLGEDGPT HQPIEHVASL RLIPNLDVWR PCDTIETAIA WQVAIERVDG
PSALVLSRQN LPQSAQDDIQ VERIRRGGYV LSEAAGGSPD VVLIATGSEV ALALDAQLAL
ADKGVRASVV SMPSTTVFDR QDAAYRADVL PAGVRRVAVE AGHSDFWHKY VGPDGRVIGL
TSFGESAPAG KLYSHFGLTV ERLYGYPSVS IDTVIGYIGH GKRELMRQVL VNLGIDAEIA
LDVVMPVFDT HYDATVGMSA QPYPGVPNAL VRLRSANIRM AVVTNKERRF AIRLLEKAGF
ESHFDVVLGG DSLPHKKPHP LPIHYCLERL TVPVHAAAHL GDSRTDVQSA RRAGVAAWAV
PYGYNHGEPI SDAQPDRIFA TIEEMADYAW SRSNGKALAP VDKGDDMTIN VAINGYGRIG
RNILRALYES KRTDEIRIVA INDLGDAKVN AHLTRYDTVH GPFAGTVDVD DDALVVNGDR
IKVLSMRNPA ELPWRALDID VVLECTGLFT SKEKASAHLV AGARKAVVHS RVERVVHD
//
