ID D8MRV9_ERWBE Unreviewed; 490 AA.
AC D8MRV9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
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:CAX59566.1};
GN OrderedLocusNames=EbC_20350 {ECO:0000313|EMBL:CAX59566.1};
OS Erwinia billingiae (strain Eb661).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634500 {ECO:0000313|EMBL:CAX59566.1, ECO:0000313|Proteomes:UP000008793};
RN [1] {ECO:0000313|EMBL:CAX59566.1, ECO:0000313|Proteomes:UP000008793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX59566.1,
RC ECO:0000313|Proteomes:UP000008793};
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(2010).
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; FP236843; CAX59566.1; -; Genomic_DNA.
DR RefSeq; WP_013202056.1; NC_014306.1.
DR AlphaFoldDB; D8MRV9; -.
DR STRING; 634500.EbC_20350; -.
DR KEGG; ebi:EbC_20350; -.
DR eggNOG; COG1070; Bacteria.
DR HOGENOM; CLU_039395_0_0_6; -.
DR UniPathway; UPA00541; UER00602.
DR Proteomes; UP000008793; 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; 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 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|HAMAP-Rule:MF_01535, ECO:0000313|EMBL:CAX59566.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01535};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01535};
KW Reference proteome {ECO:0000313|Proteomes:UP000008793};
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 7..243
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 255..440
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT ACT_SITE 237
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT BINDING 13..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT BINDING 236..238
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 402
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT DISULFID 353..370
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT DISULFID 413..417
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
SQ SEQUENCE 490 AA; 53933 MW; 69C123AF549ADF3F CRC64;
MTLRNCVAID LGASSGRVML ARFDAQTGEL QLEEVARCVN RLVTVDEQQC WDVDALETFI
TRALNTLVEQ GIVPDSIGID TWGVDYVLMD QDGERVGLPV AYRDGRTQGV MQQACQALSR
ETIYQHTGIQ FLPFNTLYQL RALTASKPEW LDRVKHALMI PDYLHYRLTG QLNWEYTNAT
TTQLLNIDSG EWDETLLAWT GAKASWFGTP SQPGTPLGNW TSADGQQVPV ISVATHDTAS
AVLAAPVAGT NAAWMSSGTW SLMGFESLEP FTGDAALALN ITNEGGAEGR YRVLKNIMGL
WLLQRVCSEL AIEDLCALID DAERQPACRS LINPNDDRFI NPTNMVREIQ DACVEQGMPA
PTDAPALARC IFDSLALFYR QVLHELEALR GHAFSWLHIV GGGCQNPLLN QLCADACGIP
VIAGPVEAST LGNIGSQLIA SGDIQDVTHL RQLIKQNFSL KTFTPHASDV YRRSWPRFQS
LTHKAKELCI
//
