RHAB_BACTN
ID RHAB_BACTN Reviewed; 485 AA.
AC Q8A1A3;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=BT_3763;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
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; AE015928; AAO78868.1; -; Genomic_DNA.
DR RefSeq; NP_812674.1; NC_004663.1.
DR RefSeq; WP_011108961.1; NC_004663.1.
DR AlphaFoldDB; Q8A1A3; -.
DR SMR; Q8A1A3; -.
DR STRING; 226186.BT_3763; -.
DR PaxDb; Q8A1A3; -.
DR PRIDE; Q8A1A3; -.
DR EnsemblBacteria; AAO78868; AAO78868; BT_3763.
DR GeneID; 60924933; -.
DR KEGG; bth:BT_3763; -.
DR PATRIC; fig|226186.12.peg.3825; -.
DR eggNOG; COG1070; Bacteria.
DR HOGENOM; CLU_039395_0_1_10; -.
DR InParanoid; Q8A1A3; -.
DR OMA; GNLLMQM; -.
DR UniPathway; UPA00541; UER00602.
DR Proteomes; UP000001414; 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; IPR000577; Carb_kinase_FGGY.
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 PIRSF; PIRSF000538; GlpK; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR02627; rhamnulo_kin; 1.
PE 3: Inferred from homology;
KW ATP-binding; Disulfide bond; Kinase; Magnesium; Nucleotide-binding;
KW Reference proteome; Rhamnose metabolism; Transferase.
FT CHAIN 1..485
FT /note="Rhamnulokinase"
FT /id="PRO_0000090530"
FT ACT_SITE 239
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 12..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 238..240
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 306
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT BINDING 404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
FT DISULFID 355..372
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01535"
SQ SEQUENCE 485 AA; 53403 MW; B29E6487F6AACB65 CRC64;
MKQNFFAVDL GATSGRTILG SFIEGGLNLE EINRFPNHLI EVGGHFYWDI YALYRHIIDG
LKLVAHRGES IASIGIDTWG VDFVLLGKDG NLLRQPYAYR DPHTVGAPEA FFSRISRSEV
YGKTGIQVMN FNSLFQLDTL RRNHDSALEA ADKVLFMPDA LSYMLTGKMV TEYTIASTAQ
LVNAHTQRLE PELLKAVGLQ EENFGRFVFP GEKIGTLTEE VQKITGLGAI PVIAVAGHDT
GSAVAAVPAL DRNFAYLSSG TWSLMGVETD APVITAETEA LNFTNEGGVE GTIRLLKNIC
GMWLLERCRL NWGDTSYPEL ITEADSCEPF RSLINPDDDC FANPADMEQA IREYCRTTGQ
PVPEQRGQIV RCIFESLALR YRQVLENLRA LSPRPIETLH VIGGGSRNDL LNQFTANAIG
IPVVAGPSEA TAIGNVMIQA MTVGEATDVA GMRQLISRSI PLKTYHPQDM AAWDAAYIHF
KNCVR
