ID A0A075K9R5_9FIRM Unreviewed; 488 AA.
AC A0A075K9R5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
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 ORFNames=UFO1_0892 {ECO:0000313|EMBL:AIF50447.1};
OS Pelosinus sp. UFO1.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Pelosinus.
OX NCBI_TaxID=484770 {ECO:0000313|EMBL:AIF50447.1, ECO:0000313|Proteomes:UP000027983};
RN [1] {ECO:0000313|EMBL:AIF50447.1, ECO:0000313|Proteomes:UP000027983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UFO1 {ECO:0000313|EMBL:AIF50447.1};
RX PubMed=25189589;
RA Brown S.D., Utturkar S.M., Magnuson T.S., Ray A.E., Poole F.L.,
RA Lancaster W.A., Thorgersen M.P., Adams M.W., Elias D.A.;
RT "Complete Genome Sequence of Pelosinus sp. Strain UFO1 Assembled Using
RT Single-Molecule Real-Time DNA Sequencing Technology.";
RL Genome Announc. 2:e00881-14(2014).
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 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; CP008852; AIF50447.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A075K9R5; -.
DR STRING; 484770.UFO1_0892; -.
DR KEGG; puf:UFO1_0892; -.
DR eggNOG; COG1070; Bacteria.
DR HOGENOM; CLU_039395_0_1_9; -.
DR UniPathway; UPA00541; UER00602.
DR Proteomes; UP000027983; 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; IPR000577; Carb_kinase_FGGY.
DR InterPro; IPR018485; FGGY_C.
DR InterPro; IPR018484; FGGY_N.
DR InterPro; IPR013449; Rhamnulokinase.
DR NCBIfam; TIGR02627; rhamnulo_kin; 1.
DR PANTHER; PTHR43095:SF2; GLUCONOKINASE; 1.
DR PANTHER; PTHR43095; SUGAR KINASE; 1.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR PIRSF; PIRSF000538; GlpK; 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|HAMAP-Rule:MF_01535};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_01535, ECO:0000313|EMBL:AIF50447.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01535};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01535};
KW Reference proteome {ECO:0000313|Proteomes:UP000027983};
KW Rhamnose metabolism {ECO:0000256|ARBA:ARBA00023308, ECO:0000256|HAMAP-
KW Rule:MF_01535};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01535, ECO:0000313|EMBL:AIF50447.1}.
FT DOMAIN 8..245
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 254..442
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT ACT_SITE 238
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT BINDING 14..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT BINDING 237..239
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT BINDING 260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT BINDING 305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT BINDING 404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT DISULFID 355..372
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
SQ SEQUENCE 488 AA; 55261 MW; B3215693A9B654DA CRC64;
MLRMKKHIAV DIGASSGRLV VGWKQEGKIQ LEEIYRFENE IRSENGSCFW NIEKLFNEIV
NGLKKAREKG IEECTLGIDT WGVDYALIDA KGNRIQEVYA YRDERTKTAI QDIRKKVSLE
EIYKKIGIQF LSFNTLFQLY VHDKEELAKA YKILLVPDYL YYRLTGIFIS EKTNASTTQL
LNLETKEYDE ELLKLIGVKR EQFATLVEPG EVIGSISELL RKQHNLPRCE LICVASHDTA
SAVIGVPGVE ECFAYLCSGT WSLMGVENMI PIANQESFCK NFTNEWGAYG TYRFLKNIMG
LWLIQEVRRN LGNKLSFAEL VSEASKISPF KFLIHCNDDC FLKPENMVLE VQNYCRNTGQ
LVPTTAGELA RCIFDSLALT YRKTLGEISS ITGYPVNCLH IVGGGVQNEL LCQLTADVVE
MPVVAGPVES TALGNIVVQM ISTGELRNLK EARNMIMNSF PIKTYQPAVI TKLDEVYHRF
NQLVSMGK
//
