RHAB_SALTY
ID RHAB_SALTY Reviewed; 489 AA.
AC P27030;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Rhamnulokinase {ECO:0000255|HAMAP-Rule:MF_01535};
DE Short=RhaB {ECO:0000255|HAMAP-Rule:MF_01535};
DE EC=2.7.1.5 {ECO:0000255|HAMAP-Rule:MF_01535};
DE AltName: Full=ATP:L-rhamnulose phosphotransferase {ECO:0000255|HAMAP-Rule:MF_01535};
DE AltName: Full=L-rhamnulose 1-kinase {ECO:0000255|HAMAP-Rule:MF_01535};
DE AltName: Full=Rhamnulose kinase {ECO:0000255|HAMAP-Rule:MF_01535};
GN Name=rhaB {ECO:0000255|HAMAP-Rule:MF_01535}; OrderedLocusNames=STM4047;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=1657713; DOI=10.1016/0378-1119(91)90511-9;
RA Nishitani J., Wilcox G.;
RT "Cloning and characterization of the L-rhamnose regulon in Salmonella
RT typhimurium LT2.";
RL Gene 105:37-42(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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:0000255|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:0000255|HAMAP-Rule:MF_01535};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01535};
CC -!- PATHWAY: Carbohydrate degradation; L-rhamnose degradation; glycerone
CC phosphate from L-rhamnose: step 2/3. {ECO:0000255|HAMAP-Rule:MF_01535}.
CC -!- SIMILARITY: Belongs to the rhamnulokinase family. {ECO:0000255|HAMAP-
CC Rule:MF_01535}.
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DR EMBL; X57299; CAA40557.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22887.1; -; Genomic_DNA.
DR PIR; JQ1289; JQ1289.
DR RefSeq; NP_462928.1; NC_003197.2.
DR RefSeq; WP_000143970.1; NC_003197.2.
DR AlphaFoldDB; P27030; -.
DR SMR; P27030; -.
DR STRING; 99287.STM4047; -.
DR PaxDb; P27030; -.
DR EnsemblBacteria; AAL22887; AAL22887; STM4047.
DR GeneID; 1255574; -.
DR KEGG; stm:STM4047; -.
DR PATRIC; fig|99287.12.peg.4264; -.
DR HOGENOM; CLU_039395_0_0_6; -.
DR OMA; MPDLFNY; -.
DR PhylomeDB; P27030; -.
DR BioCyc; SENT99287:STM4047-MON; -.
DR UniPathway; UPA00541; UER00602.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central.
DR GO; GO:0008993; F:rhamnulokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019301; P:rhamnose catabolic process; IBA:GO_Central.
DR CDD; cd07771; FGGY_RhuK; 1.
DR HAMAP; MF_01535; Rhamnulokinase; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018485; Carb_kinase_FGGY_C.
DR InterPro; IPR018484; Carb_kinase_FGGY_N.
DR InterPro; IPR013449; Rhamnulokinase.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR02627; rhamnulo_kin; 1.
PE 3: Inferred from homology;
KW ATP-binding; Disulfide bond; Kinase; Nucleotide-binding;
KW Reference proteome; Rhamnose metabolism; Transferase.
FT CHAIN 1..489
FT /note="Rhamnulokinase"
FT /id="PRO_0000090545"
FT ACT_SITE 237
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 13..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 236..238
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 259
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 402
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT DISULFID 68..222
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT DISULFID 353..370
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT DISULFID 413..417
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
SQ SEQUENCE 489 AA; 54578 MW; 47B6CB29F3397F41 CRC64;
MTFRHCVAVD LGASSGRVML ARYDSKHRTL TLREIHRFVN CLQKTDGFDT WDIDSLEKDI
RLGLKKVCNE GILIDSIGID TWGVDYVLLD KQGQRVGLPV SYRDNRTTGI MPQALVQIGK
SEIYRRSGIQ FLPFNTIYQL RALTKQQPEL TAQVAHALLM PDYFSYRLTG EMNWEYTNAT
TTQLVNINTD DWDDTLLAWT GAKKSWFGRP SHPGNVIGDW ICPQGNRIPV VAVASHDTAS
AVIASPLANK HSAYLSSGTW SLMGFESKMP YTTDEALAAN ITNEGGAEGR YRVLKNIMGL
WLLQRVLKER RITDLPALIA QTEALPACRF LINPNDDRFI NPDDMRAEIQ AACRETDQPV
PVSDAELARC IFDSLALLYA DILHEQANLR GEKFTQLHIV GGGCQNSLLN QLCADACGIR
VMAGPVEAST LGNIGIQLMT LDELNNVDDF RQVVSANYDL TTYIPNPDSE IARHVAQFQP
KRQTKELCA
