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Database: UniProt
Entry: A0A091I1R9_CALAN
LinkDB: A0A091I1R9_CALAN
Original site: A0A091I1R9_CALAN 
ID   A0A091I1R9_CALAN        Unreviewed;       896 AA.
AC   A0A091I1R9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Hexokinase-2 {ECO:0000256|ARBA:ARBA00039453};
DE            EC=2.7.1.1 {ECO:0000256|ARBA:ARBA00012324};
DE   AltName: Full=Hexokinase type II {ECO:0000256|ARBA:ARBA00041371};
DE   Flags: Fragment;
GN   ORFNames=N300_05472 {ECO:0000313|EMBL:KFP02172.1};
OS   Calypte anna (Anna's hummingbird) (Archilochus anna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC   Trochilidae; Calypte.
OX   NCBI_TaxID=9244 {ECO:0000313|EMBL:KFP02172.1, ECO:0000313|Proteomes:UP000054308};
RN   [1] {ECO:0000313|EMBL:KFP02172.1, ECO:0000313|Proteomes:UP000054308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N300 {ECO:0000313|EMBL:KFP02172.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000435};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC         Evidence={ECO:0000256|ARBA:ARBA00000435};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-hexose = ADP + D-hexose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61567, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000417};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC         Evidence={ECO:0000256|ARBA:ARBA00000417};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 1/4.
CC       {ECO:0000256|ARBA:ARBA00004888}.
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC       {ECO:0000256|ARBA:ARBA00005028}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}. Mitochondrion outer membrane
CC       {ECO:0000256|ARBA:ARBA00004450}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004450}.
CC   -!- SIMILARITY: Belongs to the hexokinase family.
CC       {ECO:0000256|ARBA:ARBA00009225}.
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DR   EMBL; KL218088; KFP02172.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091I1R9; -.
DR   STRING; 9244.A0A091I1R9; -.
DR   UniPathway; UPA00109; UER00180.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000054308; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0004396; F:hexokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019318; P:hexose metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0001678; P:intracellular glucose homeostasis; IEA:InterPro.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 2.
DR   Gene3D; 3.30.420.40; -; 2.
DR   Gene3D; 3.40.367.20; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR001312; Hexokinase.
DR   InterPro; IPR019807; Hexokinase_BS.
DR   InterPro; IPR022673; Hexokinase_C.
DR   InterPro; IPR022672; Hexokinase_N.
DR   PANTHER; PTHR19443; HEXOKINASE; 1.
DR   PANTHER; PTHR19443:SF4; HEXOKINASE-2; 1.
DR   Pfam; PF00349; Hexokinase_1; 2.
DR   Pfam; PF03727; Hexokinase_2; 2.
DR   PRINTS; PR00475; HEXOKINASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 4.
DR   PROSITE; PS00378; HEXOKINASE_1; 2.
DR   PROSITE; PS51748; HEXOKINASE_2; 2.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFP02172.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054308};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..199
FT                   /note="Hexokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00349"
FT   DOMAIN          205..439
FT                   /note="Hexokinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03727"
FT   DOMAIN          451..647
FT                   /note="Hexokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00349"
FT   DOMAIN          654..887
FT                   /note="Hexokinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03727"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP02172.1"
FT   NON_TER         896
FT                   /evidence="ECO:0000313|EMBL:KFP02172.1"
SQ   SEQUENCE   896 AA;  100227 MW;  51B8BECF87582268 CRC64;
     QIDKYLYHMR LSEETLQEVS QRFEKEMEKG LGANTNPTAV VKMLPTFVRS TPDGTEDGDF
     LALDLGGTNF RVLRVKVSDN GLQKVEMENQ IYAIPEELMR GSGVQLFDHI AECLSNFMEK
     LKIKDKKLPL GFTFSFPCYQ TKLDESILVT WTKGFKVSSV EGRDVVSLLR KSIKKRGDFD
     IDIVAVVNDT VGTMMTCGYD DHNCEIGLIV GTGTNACYME EMRHIDLVEG DEGRMCINME
     WGAFGDDGVL NDIRTEFDRE IDMGSLNPGK QLFEKMISGM YMGELVRLIL VKMTKEGLLF
     EGKLTPDLLT TGHFETRYVS AIEKEKEGLQ KAHEILSKLG LEPSHEDCVA THRICQIVST
     RSANLCGATL AAVLRRIKEN KGVERLRSTV GVDGSVYKKH PHFARRLHKT VRKLLPDCEI
     RFVRSEDGSG KGAAMVTAVA YRLAAQHKAR QKTLEALKLS HEQLLEVKQR MRIEMEKGLG
     KETHAEATVK MLPTYVCSTP DGTEKGDFLA LDLGGTNFRV LLVRVRNGMR RGVEMHNKIY
     SIPVDIMQGT GEELFDHIVH CISDFLEYMG MKGVSLPLGF TFSFPCQQTN LDEGILLKWT
     KGFKATGCEG EDVVSLLKEA IHRREEFDLD VVAVVNDTVG TMMTCGYEDP YCEVGLIVGT
     GSNACYMEEM KNVELVEGEE GRMCVNMEWG AFGDNGCLDD IRTEFDVVVD ELSLNPGKQR
     FEKMISGMYL GEIVRNILMD FTKRGLLFRG RISERLKTRG IFETKFLSQI ESDRLALLQV
     RSILQHLGLE TTCDDSIIVK EVCTVVARRA AQLCGAGMAA VVDKIRENRG LDFLKVTVGV
     DGTLYKLHPH FSTIMQETVR ELSPKCEVTF LQSEDGSGKG AALITAVACR IREAGQ
//
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