ID A0A093J4B2_DRYPU Unreviewed; 475 AA.
AC A0A093J4B2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Inositol-pentakisphosphate 2-kinase {ECO:0000256|ARBA:ARBA00014846, ECO:0000256|RuleBase:RU364126};
DE EC=2.7.1.158 {ECO:0000256|ARBA:ARBA00012023, ECO:0000256|RuleBase:RU364126};
DE Flags: Fragment;
GN ORFNames=N307_14817 {ECO:0000313|EMBL:KFV73789.1};
OS Dryobates pubescens (Downy woodpecker) (Picoides pubescens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Piciformes; Picidae; Dryobates.
OX NCBI_TaxID=118200 {ECO:0000313|EMBL:KFV73789.1, ECO:0000313|Proteomes:UP000053875};
RN [1] {ECO:0000313|EMBL:KFV73789.1, ECO:0000313|Proteomes:UP000053875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N307 {ECO:0000313|EMBL:KFV73789.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form
CC Ins(1,2,3,4,5,6)P6 (InsP6 or phytate). {ECO:0000256|RuleBase:RU364126}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-
CC inositol hexakisphosphate + ADP + H(+); Xref=Rhea:RHEA:20313,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57733,
CC ChEBI:CHEBI:58130, ChEBI:CHEBI:456216; EC=2.7.1.158;
CC Evidence={ECO:0000256|RuleBase:RU364126};
CC -!- DOMAIN: The EXKPK motif is conserved in inositol-pentakisphosphate 2-
CC kinases of both family 1 and 2. {ECO:0000256|RuleBase:RU364126}.
CC -!- SIMILARITY: Belongs to the IPK1 type 2 family.
CC {ECO:0000256|ARBA:ARBA00007229}.
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DR EMBL; KL217133; KFV73789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093J4B2; -.
DR STRING; 118200.A0A093J4B2; -.
DR Proteomes; UP000053875; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035299; F:inositol pentakisphosphate 2-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.200.110; Inositol-pentakisphosphate 2-kinase, N-lobe; 1.
DR InterPro; IPR009286; Ins_P5_2-kin.
DR InterPro; IPR043001; IP5_2-K_N_lobe.
DR PANTHER; PTHR14456; INOSITOL POLYPHOSPHATE KINASE 1; 1.
DR PANTHER; PTHR14456:SF2; INOSITOL-PENTAKISPHOSPHATE 2-KINASE; 1.
DR Pfam; PF06090; Ins_P5_2-kin; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU364126};
KW Kinase {ECO:0000256|RuleBase:RU364126, ECO:0000313|EMBL:KFV73789.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364126};
KW Reference proteome {ECO:0000313|Proteomes:UP000053875};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364126}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV73789.1"
FT NON_TER 475
FT /evidence="ECO:0000313|EMBL:KFV73789.1"
SQ SEQUENCE 475 AA; 54674 MW; 76678270948ADF19 CRC64;
LLNHCLVCVC ILECNHYFIV KSPSFFQTSE EILHHLQNIV DFGKHVMKQF FGENYVHHGE
IIQLPLDFVR QLCLKVQPER PESRCDKDMD TLSGYAMCLP NLTRLQTYRF VEHRPILCIE
IKPKCGFIPF SSHVSQEIKH KVCRYCMHQH LKVANGKWKR PSKYCPLDLF SGNKQRMHFA
LKSLLQEPQN NLKIFKNGEL IYGCKDDQDS VCDWNELARH LKPFFFPSNG LVSGPHCTRT
IVKELIHVIT MALLSSTDAC RAGDMKTVPI SQGRSYCEAS AFNKELVRNG KHKLESSGLP
RGCLLYKTLQ AQMLDMLDIE GLYPLYSRVE QYLEEFPEER STLQIDGPYN EAFYEKLLDL
STEDDGTVAF ALTKVQQYRI AMTAKDCSIM IALSPCLQDE CSEQRPVVLT SKSRFTFSVS
VLDLDLKPYE SIPHQYKLDG KIVNYYLKNV QAKDDPVMSS LFKENEDCTL VLHKV
//
