Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna03581.1-v1.0-hybrid |
Family | CBM45 |
Protein Properties | Length: 1544 Molecular Weight: 171476 Isoelectric Point: 6.193 |
Chromosome | Chromosome/Scaffold: 4 Start: 24319506 End: 24335624 |
Description | Pyruvate phosphate dikinase, PEP/pyruvate binding domain |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM45 | 253 | 328 | 2.5e-24 |
LHWGGIQDRKENWVLPSRHPDGTTVYKKKALRTPFAKSGPNSSLKIEIDDPAIQAIEFLIVDESQNRWFKNNGGNF |
Full Sequence |
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Protein Sequence Length: 1544 Download |
MASFSCYHQI SEYNGGGGFR AGNHDDGGSV EDSPYWIHAL RWVRSWGDPL YVGSFKKAKN 60 KLGKPNMSSF EFMASLVLLL SVLVRPIHIK KIEQDLVLSI NSASCAATDT VSSAPRKLPV 120 EEIKVLEEEE EDLSDCSTVT VDSSKINPSG IPANTLLRPK CVHQVPAQPR KSSLSKKFCG 180 NSLQKPKLAM GSRRPVTFVP CAVLTTDQRS DQQLASKYNL DGNIELQVYV DASSPGSTKV 240 DIHVSNSGDS LVLHWGGIQD RKENWVLPSR HPDGTTVYKK KALRTPFAKS GPNSSLKIEI 300 DDPAIQAIEF LIVDESQNRW FKNNGGNFHV KLPLKEMSIS NVSVPEDLVQ IQAYLRWERK 360 GKQMYTPEQE KASELYSRIL QIPNCHCFYI SNYNCVEYEA ARTELLEEVA RGASIQELQA 420 RLTKKSDSGN SHEQSQAGNK EVSKAAKKHE SKQVYRTGRI NRKQRDLMKI LNKHTTKPVD 480 EAKLANEESA KPKALKAVEL FAKEKEEQDG ASTLNKQIYK LGDKDLLVLV TKVADKIRVH 540 LATDIKEPVN LHWALSVNRA GEWLEPPPNV LPQGSVSLNG AVETQFVSSS VDSTYEIQSL 600 EIETQEKSFK GMPFVLCSSG NWIKNQGSDF YADFGVAVKK VQKDAGDGKG TAKALLDNIA 660 DLETDLMSQA KDAGALGLAG ILVWMRFMAT RQLIWNKNYN VKPREISKAQ DRLTDLLQSI 720 YISYPQHREL LRMILSTVGR GGEGDVGQRI RDEILVIQRN CDCKGGMMEE WHQKLHNNTS 780 PDDVVICQAL IDYIKSDFDI GVYWKTLNDN GITKERLLSY DRAIHNEPRF RADQKDRLLH 840 DLGNYLRTLK AVHSGADLES AITNCLGYSA KGQGFMVGVQ INPVSGLPSE VPGLLQFVME 900 HVEDRNVEVL VEGLLEARQE IWPLLSKPND RLKDLLFLDI ALDSTVRTAI ERGYEELNNA 960 GPEKIMYFIS MVLENLALSS DDNEDLLYCL KGWNQALNML KNNADHWALF AKSILDRTRL 1020 ALANKAELYH SILQPSAEYL GSKLGVDKLA LSIFTEEVIR AGSAASLSTL VNRLDPVLRK 1080 TANLGSWQVI SPVEVVGYVV VVDELLTVQN KVYDKPTILV ARSVRGEEEI PDGTVAVLTP 1140 DMPDVLSHVS VRARNSKVCF ATCFDSNILA DLQACEGKLL RVKPTSADVV YSEVNESELG 1200 DASSTNLNED TPALTLVKKQ FTGRYAISSD EFTSEMVGAK SRNISYIKGK LPSWVGIPTS 1260 VALPFGVFEK VLSEDSNKAV ADKIETLKKK LKEGDFGSLG EIRETVLQLT APPPLVQELK 1320 SKMQSSGMPW PGDEGEQRWE QAWLSIKKVW ASKWNERAYF STRKVKLDHD YLCMAVLVQE 1380 IINADYAFVI HTTNPSSGDS SEIYAEVVKG LGETLVGAYP GRALSFISKK NDLDSPQLLG 1440 YPSKPIGLFI RRSIIFRSDS NGEDLEGYAG AGLYDSVPMD KEEEVVLDYS SDPLVTDGNF 1500 QKKILSSIAH AGNAIEELYG LPQDIEGVIR DGKLYVVQTR PQM* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0574 | PpsA | 9.0e-12 | 1338 | 1541 | 207 | + Phosphoenolpyruvate synthase/pyruvate phosphate dikinase [Carbohydrate transport and metabolism] | ||
PRK06241 | PRK06241 | 6.0e-12 | 1345 | 1541 | 203 | + phosphoenolpyruvate synthase; Validated | ||
TIGR01418 | PEP_synth | 4.0e-14 | 1235 | 1542 | 345 | + phosphoenolpyruvate synthase. Also called pyruvate,water dikinase and PEP synthase. The member from Methanococcus jannaschii contains a large intein. This enzyme generates phosphoenolpyruvate (PEP) from pyruvate, hydrolyzing ATP to AMP and releasing inorganic phosphate in the process. The enzyme shows extensive homology to other enzymes that use PEP as substrate or product. This enzyme may provide PEP for gluconeogenesis, for PTS-type carbohydrate transport systems, or for other processes [Energy metabolism, Glycolysis/gluconeogenesis]. | ||
PRK06464 | PRK06464 | 4.0e-14 | 1346 | 1541 | 209 | + phosphoenolpyruvate synthase; Validated | ||
pfam01326 | PPDK_N | 2.0e-30 | 1233 | 1542 | 335 | + Pyruvate phosphate dikinase, PEP/pyruvate binding domain. This enzyme catalyzes the reversible conversion of ATP to AMP, pyrophosphate and phosphoenolpyruvate (PEP). |
Gene Ontology | |
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GO Term | Description |
GO:0005524 | ATP binding |
GO:0016301 | kinase activity |
GO:0016310 | phosphorylation |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2ols_A | 0.003 | 1345 | 1542 | 157 | 336 | A Chain A, The Crystal Structure Of The Phosphoenolpyruvate Synthase From Neisseria Meningitidis |
Sequence Alignments (This image is cropped. Click for full image.) |
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