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Database: UniProt
Entry: A0A0Q5VN36_9ACTN
LinkDB: A0A0Q5VN36_9ACTN
Original site: A0A0Q5VN36_9ACTN 
ID   A0A0Q5VN36_9ACTN        Unreviewed;       450 AA.
AC   A0A0Q5VN36;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Carbohydrate kinase {ECO:0000313|EMBL:KQS58622.1};
GN   ORFNames=ASG36_11340 {ECO:0000313|EMBL:KQS58622.1};
OS   Geodermatophilus sp. Leaf369.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=1736354 {ECO:0000313|EMBL:KQS58622.1, ECO:0000313|Proteomes:UP000051830};
RN   [1] {ECO:0000313|EMBL:KQS58622.1, ECO:0000313|Proteomes:UP000051830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf369 {ECO:0000313|EMBL:KQS58622.1,
RC   ECO:0000313|Proteomes:UP000051830};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS58622.1, ECO:0000313|Proteomes:UP000051830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf369 {ECO:0000313|EMBL:KQS58622.1,
RC   ECO:0000313|Proteomes:UP000051830};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family.
CC       {ECO:0000256|RuleBase:RU003733}.
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:KQS58622.1}.
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DR   EMBL; LMQA01000002; KQS58622.1; -; Genomic_DNA.
DR   RefSeq; WP_055763808.1; NZ_LMQA01000002.1.
DR   AlphaFoldDB; A0A0Q5VN36; -.
DR   STRING; 1736354.ASG36_11340; -.
DR   OrthoDB; 9782710at2; -.
DR   Proteomes; UP000051830; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR   GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
DR   InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR   InterPro; IPR018485; FGGY_C.
DR   InterPro; IPR018484; FGGY_N.
DR   PANTHER; PTHR43095; SUGAR KINASE; 1.
DR   PANTHER; PTHR43095:SF6; XYLULOSE KINASE; 1.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   PIRSF; PIRSF000538; GlpK; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00445; FGGY_KINASES_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022629};
KW   Kinase {ECO:0000256|RuleBase:RU003733, ECO:0000313|EMBL:KQS58622.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051830};
KW   Transferase {ECO:0000256|RuleBase:RU003733};
KW   Xylose metabolism {ECO:0000256|ARBA:ARBA00022629}.
FT   DOMAIN          5..237
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          247..425
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
SQ   SEQUENCE   450 AA;  45094 MW;  E62E9BFE4F1A8954 CRC64;
     MSDLLLGADL GTSGLKLAAL DTAGAVVAEA EVAYPVDTPR QGWAQTEVAV WRSALDEALA
     QLTPALAGHA VRGLGLSGQM HGAVLVDDAG AALAPALLWP DQRAAAQVER WRALPDADRA
     ALANPLVPGM TGPLVAWLAE HEPELVARAA GVLLPKDALR ATLLPGVDPA VTDRSDAAAT
     LLWDVPADDW SAAAVGLAGV RCPRVLPSHA VAGTAVLPGI GEVPVVVGGA DTPLALLATG
     TSTGLQVNLG TGAQLLRPGA TPAPALDPVV HTYADAEQGW YAMAALQNGG LAWDWVRRVL
     GFGWEELLAT LDGSAPGAGG VRFAPWLTGE RGGVAGPTDR GAWTGLHPGT TRADLGRAAL
     EGVAAAVAAG AGLLDVAGDE PVVLTGGGAR TPAVQQLLAD ALGRPVQLVQ VRSASATGAA
     LLAARGVGLS CTPQRVLGPV VDPRGVSASG
//
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