ID A0A091EX94_CORBR Unreviewed; 465 AA.
AC A0A091EX94;
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=N302_07221 {ECO:0000313|EMBL:KFO60949.1};
OS Corvus brachyrhynchos (American crow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC Corvus.
OX NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO60949.1, ECO:0000313|Proteomes:UP000052976};
RN [1] {ECO:0000313|EMBL:KFO60949.1, ECO:0000313|Proteomes:UP000052976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO60949.1};
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; KK719041; KFO60949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091EX94; -.
DR STRING; 85066.A0A091EX94; -.
DR Proteomes; UP000052976; 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:KFO60949.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364126};
KW Reference proteome {ECO:0000313|Proteomes:UP000052976};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364126}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO60949.1"
FT NON_TER 465
FT /evidence="ECO:0000313|EMBL:KFO60949.1"
SQ SEQUENCE 465 AA; 53547 MW; 38E6485E103358E7 CRC64;
QRCVVLRFLK SPPNQNKTPE EILHHLQNIV DFGKHVMKQF FGENDVHHGE IIQLPLDFVR
QLCLKIQPER PECRCDKDMD TLSGYAMCLP NLTRLQTFRF AEHRPILCIE IKPKCGFIPF
SSHVSQEIKH KVCRYCMHQH LKVANGKWKR PSKYCPLDLF SGNKQRMHFA LKSLLQEAQN
NLKIFKNGEL IYGCKDDQDC VSDWNELARH LKPFFFPSNG LVSGPHCTRT IVKELIHVIT
MALLSSTDTC RAGDMKTVPI SQGRSYCEAS AFNKELVRNG KHKLESSGLP RGCLLYKTLQ
AQMLDMLDIE GLYPLYSRVE QYLEEFPEER STLQIDGPYN EVFYEKLLDL SLEDDGTVAF
ALTKVQQYRI AMTAKDCSIM IALSPCLQDE CSEHRPVVLT SKSRFTFSVS VLDLDLKPYE
SIPHQYKLDG EIVNYYLKNV QAKEDPVMSS LFKENEDCTL VLHKV
//