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Database: UniProt
Entry: A0A1M3HNS2_9SPHI
LinkDB: A0A1M3HNS2_9SPHI
Original site: A0A1M3HNS2_9SPHI 
ID   A0A1M3HNS2_9SPHI        Unreviewed;       328 AA.
AC   A0A1M3HNS2;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Glucokinase {ECO:0000313|EMBL:OJW60180.1};
GN   ORFNames=BGO55_17055 {ECO:0000313|EMBL:OJW60180.1};
OS   Sphingobacteriales bacterium 50-39.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1895841 {ECO:0000313|EMBL:OJW60180.1, ECO:0000313|Proteomes:UP000184242};
RN   [1] {ECO:0000313|EMBL:OJW60180.1, ECO:0000313|Proteomes:UP000184242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=50-39 {ECO:0000313|EMBL:OJW60180.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family.
CC       {ECO:0000256|ARBA:ARBA00006479}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OJW60180.1}.
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DR   EMBL; MKTZ01000002; OJW60180.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3HNS2; -.
DR   STRING; 1895841.BGO55_17055; -.
DR   Proteomes; UP000184242; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000600; ROK.
DR   PANTHER; PTHR18964:SF149; BIFUNCTIONAL UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE_N-ACETYLMANNOSAMINE KINASE; 1.
DR   PANTHER; PTHR18964; ROK (REPRESSOR, ORF, KINASE) FAMILY; 1.
DR   Pfam; PF00480; ROK; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR   PROSITE; PS01125; ROK; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:OJW60180.1};
KW   Transferase {ECO:0000313|EMBL:OJW60180.1}.
SQ   SEQUENCE   328 AA;  34738 MW;  3231F8EFF0497587 CRC64;
     MAKAASSSSY ESLAIGIDIG GTGTKFGIVD RIGNVLFSSE ISTRGHSQVE SFIDELHSHL
     SVLIEKAGGT GRMRGIGVGA PNGNYYSGTV EYAPNLPWRG IIPLAKLIQN KFQLPTILTN
     DANAAAIGEM MYGAAKGMKD FIMITLGTGV GSGIVANGKL IYGHDGFAGE LGHTIIIPHG
     RLHEGTGKKG SLESYASATG VKLTAIEMLE KSQEASLLRG IPKNQLDSKK VYDAAIQGDK
     LAKAIFDFTG EILGLALANF VMFSSPEAII LFGGLTKSGD LILKPTRENM ESNLIQVFQN
     KVKILVSHLK ESDAAILGAS ALVWDMKI
//
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