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
//