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Database: UniProt
Entry: A0A385NJW5_9BACI
LinkDB: A0A385NJW5_9BACI
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ID   A0A385NJW5_9BACI        Unreviewed;       473 AA.
AC   A0A385NJW5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Rhamnulokinase {ECO:0000256|HAMAP-Rule:MF_01535};
DE            Short=RhaB {ECO:0000256|HAMAP-Rule:MF_01535};
DE            EC=2.7.1.5 {ECO:0000256|HAMAP-Rule:MF_01535};
DE   AltName: Full=ATP:L-rhamnulose phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01535};
DE   AltName: Full=L-rhamnulose 1-kinase {ECO:0000256|HAMAP-Rule:MF_01535};
DE   AltName: Full=Rhamnulose kinase {ECO:0000256|HAMAP-Rule:MF_01535};
GN   Name=rhaB {ECO:0000256|HAMAP-Rule:MF_01535,
GN   ECO:0000313|EMBL:AYA74434.1};
GN   ORFNames=DOE78_02640 {ECO:0000313|EMBL:AYA74434.1};
OS   Bacillus sp. Y1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=352858 {ECO:0000313|EMBL:AYA74434.1, ECO:0000313|Proteomes:UP000265711};
RN   [1] {ECO:0000313|EMBL:AYA74434.1, ECO:0000313|Proteomes:UP000265711}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y1 {ECO:0000313|EMBL:AYA74434.1};
RA   Rathod J., Jean J.-S.;
RT   "Arsenic resistant and redox active subsurface bacterial isolate Bacillus
RT   sp. Y1 from Yichu borehole sediment.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose).
CC       Catalyzes the transfer of the gamma-phosphate group from ATP to the 1-
CC       hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01535}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-rhamnulose = ADP + H(+) + L-rhamnulose 1-phosphate;
CC         Xref=Rhea:RHEA:20117, ChEBI:CHEBI:15378, ChEBI:CHEBI:17897,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58313, ChEBI:CHEBI:456216; EC=2.7.1.5;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01535};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01535};
CC   -!- PATHWAY: Carbohydrate degradation; L-rhamnose degradation; glycerone
CC       phosphate from L-rhamnose: step 2/3. {ECO:0000256|HAMAP-Rule:MF_01535}.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family.
CC       {ECO:0000256|ARBA:ARBA00009156}.
CC   -!- SIMILARITY: Belongs to the rhamnulokinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01535}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01535}.
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DR   EMBL; CP030028; AYA74434.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A385NJW5; -.
DR   KEGG; bacq:DOE78_02640; -.
DR   OrthoDB; 9761504at2; -.
DR   UniPathway; UPA00541; UER00602.
DR   Proteomes; UP000265711; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008993; F:rhamnulokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019301; P:rhamnose catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07771; FGGY_RhuK; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_01535; Rhamnulokinase; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
DR   InterPro; IPR018485; FGGY_C.
DR   InterPro; IPR018484; FGGY_N.
DR   InterPro; IPR013449; Rhamnulokinase.
DR   NCBIfam; TIGR02627; rhamnulo_kin; 1.
DR   PANTHER; PTHR10196:SF93; L-RHAMNULOKINASE; 1.
DR   PANTHER; PTHR10196; SUGAR KINASE; 1.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   PIRSF; PIRSF000538; GlpK; 2.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01535};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW   Rule:MF_01535};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01535};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01535};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01535};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265711};
KW   Rhamnose metabolism {ECO:0000256|ARBA:ARBA00023308, ECO:0000256|HAMAP-
KW   Rule:MF_01535};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01535}.
FT   DOMAIN          4..244
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          254..441
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
FT   ACT_SITE        238
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT   BINDING         12..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT   BINDING         80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT   BINDING         237..239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT   BINDING         259
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT   BINDING         296
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT   BINDING         304
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT   BINDING         403
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT   DISULFID        354..371
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
SQ   SEQUENCE   473 AA;  53881 MW;  66EE8052C1FA8F21 CRC64;
     MNKYSIAVDI GASSGRLMLG HRENGHLQLR ELYRFENKIV QKGNYFCWEL DRLFDEIKTG
     LKKCRELGIQ PDSIGIDTWA VDFVLLDEND QPLTEAVSYR DPRTDGMMEE VFELISKERL
     YLETGIQFQK FNTIYQLYSL KKNHPDILAK AKSFLMIPDY LNFLLTGNKS NEYTNATSTQ
     LVNAFTKKWD YELLDILGIN KDMFHEIQLP KTILGNLKEE LVSELGFDMN VILPATHDTG
     SAVISVPEEE STIYISSGTW SLMGTENHFP ICVTKALDYN FTNEGGIDYR FRFLKNIMGL
     WMIQEVKRNY DHEYTFAKLV ELAEEAGDFQ SIVNVNDDRF LKPENMIQEI MNYCIETGQR
     VPSKPGEVAK CVYDSLASSY KETIGEIESI FEKSFDKINV IGGGCQNEML NQLVADVTNK
     EVLAGPIEAT AIGNIVAQLM ALGEFTDLQE VRSVIKQSFE VKKYEPTKSV ANS
//
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