Reviewed, UniProtKB/Swiss-Prot A2PYL7 (HXK2_EQUZE)

Names and origin

Protein names

Recommended name:
    Hexokinase-2
    EC=2.7.1.1
Alternative name(s):
    Hexokinase type II
      Short name=HK II

Gene names

Name:

HK2

Organism

Equus zebra (Mountain zebra)

Taxonomic identifier

9791 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus

Protein attributes

Sequence length	917 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	ATP + D-hexose = ADP + D-hexose 6-phosphate.
Enzyme regulation	Hexokinase is an allosteric enzyme inhibited by its product Glc-6-P By similarity.
Pathway	Carbohydrate metabolism; hexose metabolism.
Subunit structure	Monomer By similarity.
Domain	The N- and C-terminal halves of this hexokinase show extensive sequence similarity to each other. The catalytic activity is associated with the C-terminus while regulatory function is associated with the N-terminus.
Miscellaneous	In vertebrates there are four major glucose-phosphorylating isoenzymes, designated hexokinase I, II, III and IV (glucokinase).
Sequence similarities	Belongs to the hexokinase family.

Ontologies

Keywords
Biological process	Glycolysis
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Allosteric enzyme
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW hexokinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 917	917	Hexokinase-2		PRO_0000286050
Regions
	Nucleotide binding	84 – 89	6	ATP 1 Potential
	Nucleotide binding	425 – 426	2	ATP 1 By similarity
	Nucleotide binding	532 – 537	6	ATP 2 By similarity
	Nucleotide binding	747 – 748	2	ATP 2 By similarity
	Nucleotide binding	784 – 788	5	ATP 2 By similarity
	Nucleotide binding	863 – 867	5	ATP 2 By similarity
	Region	1 – 12	12	Hydrophobic
	Region	13 – 475	463	Regulatory
	Region	84 – 88	5	Glucose-6-phosphate 1 binding By similarity
	Region	155 – 156	2	Substrate 1 binding By similarity
	Region	172 – 173	2	Substrate 1 binding By similarity
	Region	208 – 209	2	Substrate 1 binding By similarity
	Region	291 – 294	4	Substrate 1 binding By similarity
	Region	413 – 415	3	Glucose-6-phosphate 1 binding By similarity
	Region	476 – 917	442	Catalytic
	Region	532 – 536	5	Glucose-6-phosphate 2 binding By similarity
	Region	603 – 604	2	Substrate 2 binding By similarity
	Region	620 – 621	2	Substrate 2 binding By similarity
	Region	656 – 657	2	Substrate 2 binding By similarity
	Region	739 – 742	4	Substrate 2 binding By similarity
	Region	861 – 863	3	Glucose-6-phosphate 2 binding By similarity
Sites
	Binding site	30	1	ATP 1 By similarity
	Binding site	209	1	Glucose-6-phosphate 1 By similarity
	Binding site	235	1	Substrate 1 By similarity
	Binding site	260	1	Substrate 1 By similarity
	Binding site	449	1	Glucose-6-phosphate 1 By similarity
	Binding site	558	1	ATP 2 Potential
	Binding site	657	1	Glucose-6-phosphate 2 By similarity
	Binding site	680	1	ATP 2 By similarity
	Binding site	680	1	Glucose-6-phosphate 2 By similarity
	Binding site	683	1	Substrate 2 By similarity
	Binding site	708	1	Substrate 2 By similarity
	Binding site	897	1	Glucose-6-phosphate 2 By similarity
Amino acid modifications
	Modified residue	461	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A2PYL7-1 [UniParc]. Last modified March 6, 2007. Version 1. Checksum: 65C12AFAB051F95F	FASTA	917	102,654
	10 20 30 40 50 60 MIASHLLAYF FTELNHDQVQ KVDQYLYHMR LSDETLLEIS KRFRKEMEKG LAATTHPTAS 70 80 90 100 110 120 VKMLPTFVRS TPDGTEHGEF LALDLGGTNF RVLRVRVTDN GLQKVEMENQ IYAIPEDIMQ 130 140 150 160 170 180 GSGTQLFDHI AGCLANFMDK LQIKDKKLPL GFTFSFPCIQ TKLDESFLVS WTKGFKSRGV 190 200 210 220 230 240 EGRDVVTLIR KAIQRRGDFD IDIVAMVNDT VATMMTCGYD DQNCEIGLIV GMGSNACYME 250 260 270 280 290 300 EMRYIDTVEG DEGRMCINME WGAFGDDGTL DDIRTEFDQE IDMGSLNPGQ QLFEKMISGM 310 320 330 340 350 360 YMGELVRLIL VKMAKEELLF RGKLSPELLT TGRFETKDVS EIEGEKDGIQ KAREVLVRLG 370 380 390 400 410 420 MDPTQEDCVA THRICQIVST RSASLCAATL AAVLQRIKEN KGEERLRSTI GVDGSVYKKH 430 440 450 460 470 480 PHFAKRLQKT VRRLVPNCDI RFLCSEDGSG KGAAMVTAVA YRLAYQHRAR LKTLEPLKLS 490 500 510 520 530 540 REQLLEVKRR MKVEMERGLS KETHASAPVK MLPTYVCATP DGTEKGDFLA LDLGGTNFRV 550 560 570 580 590 600 LLVRVRNGKR RGVEMHNKIY SIPQDIMHGT GDELFDHIVQ CIADFLEYMG MKGVSLPLGF 610 620 630 640 650 660 TFSFPCQQNR LDESILLKWT KGFKASGCEG EDVVTLLKEA IHRREEFDLD VVAVVNDTVG 670 680 690 700 710 720 TMMTCGYEDP HCEVGLIVGT GSNACYMEEM RNVELVEGEE GRMCVNTEWG AFGDNGCLDD 730 740 750 760 770 780 FCTEFDVAVD ELSLNPGKQR FEKMMSGMYL GEIVRNILID FTKRGLLFRG RISERLKTRG 790 800 810 820 830 840 IFETKFLSQI ESDCLALQQV RAILQHLGLE STCDDSIIVK EVCTVVAQRA AQLCGAGMAA 850 860 870 880 890 900 VVDKIRENRG LDTLKVTVGV DGTLYKLHPH FAKVMRETVK DLAPKCDVSF LESEDGSGKG 910 AALITAVACR IREAGQR

References

[1]	"Sequencing of cDNA and proximal promoter of equine hexokinase II gene." Sato T., Itou T., Sato G., Kobayashi Y., Endo H., Sakai T. DNA Seq. 18:203-208(2007) [PubMed: 17454005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Skeletal muscle.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB248869 mRNA. Translation: BAF45851.1.
3D structure databases
SMR	A2PYL7. Positions 17-913.
ModBase	Search...
Phylogenomic databases
HOVERGEN	A2PYL7.
Enzyme and pathway databases
BRENDA	2.7.1.1. 300296.
Family and domain databases
InterPro	IPR001312. Hexokinase. IPR019807. Hexokinase_CS. [Graphical view]
PANTHER	PTHR19443. Hexokinase. 1 hit.
Pfam	PF00349. Hexokinase_1. 2 hits. PF03727. Hexokinase_2. 2 hits. [Graphical view]
PRINTS	PR00475. HEXOKINASE.
PROSITE	PS00378. HEXOKINASES. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HXK2_EQUZE

Accession

Primary (citable) accession number: A2PYL7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 2007
Last sequence update:	March 6, 2007
Last modified:	January 19, 2010
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)