RHAB_ECOUT
ID RHAB_ECOUT Reviewed; 489 AA.
AC Q1R415;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Rhamnulokinase {ECO:0000255|HAMAP-Rule:MF_01535, ECO:0000303|PubMed:17568582};
DE EC=2.7.1.5 {ECO:0000255|HAMAP-Rule:MF_01535, ECO:0000269|PubMed:17568582};
DE AltName: Full=Rhamnulose kinase {ECO:0000255|HAMAP-Rule:MF_01535, ECO:0000303|PubMed:17568582};
GN Name=rhaB {ECO:0000255|HAMAP-Rule:MF_01535, ECO:0000303|PubMed:17568582};
GN OrderedLocusNames=UTI89_C4487;
OS Escherichia coli (strain UTI89 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=364106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTI89 / UPEC;
RX PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA Gordon J.I.;
RT "Identification of genes subject to positive selection in uropathogenic
RT strains of Escherichia coli: a comparative genomics approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND
RP ADP, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=17568582; DOI=10.1016/j.febslet.2007.05.075;
RA Grueninger D., Schulz G.E.;
RT "Substrate spectrum of L-rhamnulose kinase related to models derived from
RT two ternary complex structures.";
RL FEBS Lett. 581:3127-3130(2007).
CC -!- FUNCTION: Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose).
CC It could also play a role in the metabolism of some rare sugars such as
CC L-fructose. Catalyzes the transfer of the gamma-phosphate group from
CC ATP to the 1-hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-
CC phosphate. It can also phosphorylate L-fuculose and L-xylulose. It
CC requires the R-configuration at the C-3 atom. {ECO:0000255|HAMAP-
CC Rule:MF_01535, ECO:0000269|PubMed:17568582}.
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 ECO:0000269|PubMed:17568582};
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 -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01535,
CC ECO:0000269|PubMed:17568582}.
CC -!- SIMILARITY: Belongs to the rhamnulokinase family. {ECO:0000255|HAMAP-
CC Rule:MF_01535}.
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DR EMBL; CP000243; ABE09899.1; -; Genomic_DNA.
DR RefSeq; WP_000144110.1; NC_007946.1.
DR PDB; 2UYT; X-ray; 1.55 A; A=1-489.
DR PDBsum; 2UYT; -.
DR AlphaFoldDB; Q1R415; -.
DR SMR; Q1R415; -.
DR EnsemblBacteria; ABE09899; ABE09899; UTI89_C4487.
DR KEGG; eci:UTI89_C4487; -.
DR HOGENOM; CLU_039395_0_0_6; -.
DR OMA; MPDLFNY; -.
DR UniPathway; UPA00541; UER00602.
DR EvolutionaryTrace; Q1R415; -.
DR Proteomes; UP000001952; Chromosome.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0008993; F:rhamnulokinase activity; IDA:UniProtKB.
DR GO; GO:0019301; P:rhamnose catabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Disulfide bond; Kinase; Magnesium;
KW Nucleotide-binding; Rhamnose metabolism; Transferase.
FT CHAIN 1..489
FT /note="Rhamnulokinase"
FT /id="PRO_0000297519"
FT ACT_SITE 237
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535,
FT ECO:0000269|PubMed:17568582"
FT BINDING 13..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535,
FT ECO:0000269|PubMed:17568582"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535,
FT ECO:0000269|PubMed:17568582"
FT BINDING 236..238
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535,
FT ECO:0000269|PubMed:17568582"
FT BINDING 259
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535,
FT ECO:0000269|PubMed:17568582"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535,
FT ECO:0000269|PubMed:17568582"
FT BINDING 304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535,
FT ECO:0000269|PubMed:17568582"
FT BINDING 402
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535,
FT ECO:0000269|PubMed:17568582"
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"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:2UYT"
FT STRAND 13..24
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:2UYT"
FT STRAND 29..39
FT /evidence="ECO:0007829|PDB:2UYT"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:2UYT"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 53..69
FT /evidence="ECO:0007829|PDB:2UYT"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:2UYT"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:2UYT"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 110..118
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 120..127
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 136..146
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:2UYT"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:2UYT"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:2UYT"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 194..200
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:2UYT"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:2UYT"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 237..244
FT /evidence="ECO:0007829|PDB:2UYT"
FT STRAND 252..269
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 274..279
FT /evidence="ECO:0007829|PDB:2UYT"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:2UYT"
FT STRAND 291..297
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 315..322
FT /evidence="ECO:0007829|PDB:2UYT"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 345..355
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 364..390
FT /evidence="ECO:0007829|PDB:2UYT"
FT STRAND 395..401
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 402..405
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 407..417
FT /evidence="ECO:0007829|PDB:2UYT"
FT STRAND 419..423
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 428..440
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 447..457
FT /evidence="ECO:0007829|PDB:2UYT"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:2UYT"
FT HELIX 470..477
FT /evidence="ECO:0007829|PDB:2UYT"
SQ SEQUENCE 489 AA; 54076 MW; E2B573E7AE58CA24 CRC64;
MTFRNCVAVD LGASSGRVML ARYERECRSL TLREIHRFNN GLHSQNGYVT WNVDSLESAI
RLGLNKVCEE GIRIDSIGID TWGVDFVLLD QQGQRVGLPV AYRDSRTNGL MAQAQQQLGK
RDIYQRSGIQ FLPFNTIYQL RALTEQQPEL IPHIAHALLI PDYFSYRLTG KMNWEYTNAT
TTQLVNINSD DWDESLLAWS GANKAWFGRP THPGNVIGHW ICPQGNEIPV VAVASHDTAS
AVIASPLNGS RAAYLSSGTW SLMGFESQTP FTNDTALAAN ITNEGGAEGR YRVLKNIMGL
WLLQRVLQER QINDLPALIA ATQALPACRF IINPNDDRFI NPDEMCSEIQ AACRETAQPI
PESDAELARC IFDSLALLYA DVLHELAQLR GEDFSQLHIV GGGCQNTLLN QLCADACGIR
VIAGPVEAST LGNIGIQLMT LDELNNVDDF RQVVSTTANL TTFTPNPDSE IAHYVAQIHS
TRQTKELCA
