ID   RHAB_MANSM              Reviewed;         482 AA.
AC   Q65Q24;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=MS2329;
OS   Mannheimia succiniciproducens (strain MBEL55E).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Basfia.
OX   NCBI_TaxID=221988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBEL55E;
RX   PubMed=15378067; DOI=10.1038/nbt1010;
RA   Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA   Jeong H., Hur C.G., Kim J.J.;
RT   "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT   succiniciproducens.";
RL   Nat. Biotechnol. 22:1275-1281(2004).
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; AE016827; AAU38936.1; -; Genomic_DNA.
DR   RefSeq; WP_011201474.1; NC_006300.1.
DR   AlphaFoldDB; Q65Q24; -.
DR   SMR; Q65Q24; -.
DR   STRING; 221988.MS2329; -.
DR   EnsemblBacteria; AAU38936; AAU38936; MS2329.
DR   KEGG; msu:MS2329; -.
DR   eggNOG; COG1070; Bacteria.
DR   HOGENOM; CLU_039395_0_0_6; -.
DR   OMA; MPDLFNY; -.
DR   OrthoDB; 1619686at2; -.
DR   UniPathway; UPA00541; UER00602.
DR   Proteomes; UP000000607; 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   HAMAP; MF_01535; Rhamnulokinase; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018484; Carb_kinase_FGGY_N.
DR   InterPro; IPR013449; Rhamnulokinase.
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   Rhamnose metabolism; Transferase.
FT   CHAIN           1..482
FT                   /note="Rhamnulokinase"
FT                   /id="PRO_0000090540"
FT   ACT_SITE        233
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         232..234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT   BINDING         255
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT   BINDING         292
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT   BINDING         300
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT   BINDING         398
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT   DISULFID        349..366
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT   DISULFID        409..413
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
SQ   SEQUENCE   482 AA;  53707 MW;  514194AC2AD47290 CRC64;
     MTILNIAAVD LGASSGRVML ASYSTENHKI SLEEIHRFKN QFVSQNGHEC WDLAYLENEI
     VNGLRKISNS GRTLHSIGID TWGVDYVLLD QNGEVVGPTY AYRDHRTDGV MQKVQAELGK
     EVIYRKTGIQ FLTFNTLYQL KAMTDENPAW LSQVKDFVMI PDYLNYRLTG VINREYTNAT
     TTQLVNVNID SWDTALLDYL GLPASWFGRI RHPGHQVGLW ENRVPVMSVA SHDTASAVIS
     APLSDENAAY LCSGTWSLMG LDTTTPCTDE CAMNANITNE GGIDGHYRVL KNIMGLWLFN
     RLCTERDVTD IPALVKQAEA ELPFQSLINP NAECFLNPSS MVEAIQQYCR EHNQVIPKTT
     AQLARCIFDS LAMLYRKVAL ELAGLQGKPI SALHIVGGGS QNAFLNQLCA DLCGIDVFAG
     PVEASVLGNV GCQLMALDQI HNAAEFRQLV VKNFPLKQFK KRPHFMPASD FEEKWCEFCA
     LN