ID   G7K998_MEDTR            Unreviewed;       496 AA.
AC   G7K998;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE            EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN   Name=11426910 {ECO:0000313|EnsemblPlants:AES93923};
GN   OrderedLocusNames=MTR_5g009000 {ECO:0000313|EMBL:AES93923.1};
GN   ORFNames=MtrunA17_Chr5g0396421 {ECO:0000313|EMBL:RHN53492.1};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880 {ECO:0000313|EMBL:AES93923.1, ECO:0000313|Proteomes:UP000002051};
RN   [1] {ECO:0000313|EMBL:AES93923.1, ECO:0000313|Proteomes:UP000002051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A17 {ECO:0000313|EMBL:AES93923.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:AES93923,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=22089132; DOI=10.1038/nature10625;
RA   Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA   Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA   Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA   Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA   Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA   Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA   Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA   Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA   Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA   Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA   Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA   Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA   Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA   Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA   Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA   Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA   Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA   Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA   Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA   Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA   Town C.D., Roe B.A.;
RT   "The Medicago genome provides insight into the evolution of rhizobial
RT   symbioses.";
RL   Nature 480:520-524(2011).
RN   [2] {ECO:0000313|EMBL:AES93923.1, ECO:0000313|Proteomes:UP000002051}
RP   GENOME REANNOTATION.
RC   STRAIN=A17 {ECO:0000313|EMBL:AES93923.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:AES93923,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA   Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA   Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA   Schwartz D.C., Town C.D.;
RT   "An improved genome release (version Mt4.0) for the model legume Medicago
RT   truncatula.";
RL   BMC Genomics 15:312-312(2014).
RN   [3] {ECO:0000313|EnsemblPlants:AES93923}
RP   IDENTIFICATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES93923};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
RN   [4] {ECO:0000313|EMBL:RHN53492.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:RHN53492.1};
RA   Pecrix Y., Gamas P., Carrere S.;
RT   "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL   Nat. Plants 0:0-0(2018).
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   -!- SIMILARITY: Belongs to the hexokinase family.
CC       {ECO:0000256|ARBA:ARBA00009225, ECO:0000256|RuleBase:RU362007}.
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DR   EMBL; CM001221; AES93923.1; -; Genomic_DNA.
DR   EMBL; PSQE01000005; RHN53492.1; -; Genomic_DNA.
DR   RefSeq; XP_003610965.1; XM_003610917.2.
DR   AlphaFoldDB; G7K998; -.
DR   STRING; 3880.G7K998; -.
DR   PaxDb; 3880-AES93923; -.
DR   EnsemblPlants; AES93923; AES93923; MTR_5g009000.
DR   GeneID; 11426910; -.
DR   Gramene; AES93923; AES93923; MTR_5g009000.
DR   KEGG; mtr:11426910; -.
DR   eggNOG; KOG1369; Eukaryota.
DR   HOGENOM; CLU_014393_5_1_1; -.
DR   OMA; ADCVQQF; -.
DR   OrthoDB; 5481886at2759; -.
DR   UniPathway; UPA00109; UER00180.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000002051; Chromosome 5.
DR   Proteomes; UP000265566; Chromosome 5.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004340; F:glucokinase activity; IEA:UniProt.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
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; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.40.367.20; -; 1.
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:SF6; HEXOKINASE-4; 1.
DR   Pfam; PF00349; Hexokinase_1; 1.
DR   Pfam; PF03727; Hexokinase_2; 1.
DR   PRINTS; PR00475; HEXOKINASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00378; HEXOKINASE_1; 1.
DR   PROSITE; PS51748; HEXOKINASE_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362007};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU362007};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362007};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362007};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}.
FT   DOMAIN          41..238
FT                   /note="Hexokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00349"
FT   DOMAIN          245..493
FT                   /note="Hexokinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03727"
SQ   SEQUENCE   496 AA;  53978 MW;  26EEF61D2CAA170F CRC64;
     MGRVVVGVTA TVAVAACAVA AVIVARRVKS RRKWKKVANV LKEFEEGCDT SVGRLRQVVD
     AMAVEMHAGL ASEGGSKLKM LLTYVDNLPN GTEKGPYYAL HLGGTNFRVT RVHLSGQPSP
     VLEHEVERQP IPPHLMTGTS KDLFDFIASS LKEFVAKEDG SNSSQDRREL GFTFSFPMKQ
     MSVSSGILIK WTKGFSIVDM VGRDVAACLQ EAFARNGLDV HVAALVNDTV GTLAVGHYHD
     PDTVAAIVIG TGTNACYLER IDAIIKCQGL LTTSGRMVVN MEWGNFWSSH LPRTQYDIEL
     DAESPNPNDQ GFEKMISGMY LGDIVRRVIL RMSLESDMFE PISSKLLTPF ILRTPLMAAM
     HEDDSPDLIE VARILNDTFE IPDLPLKARK IVVKVCDVVT RRAARLAAAG IVGILKKIGR
     DGSGGITGGR SRSDIKMKRT VVAIEGGLYS SYTLFREYLH EALNEILGED IAKHVILNVT
     EDGSGIGAAL LAASYS
//