ID A0A090ZIV4_PAEMA Unreviewed; 489 AA.
AC A0A090ZIV4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
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:KFN10175.1};
GN ORFNames=DJ90_440 {ECO:0000313|EMBL:KFN10175.1}, GNQ08_24455
GN {ECO:0000313|EMBL:MUG25519.1};
OS Paenibacillus macerans (Bacillus macerans).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=44252 {ECO:0000313|EMBL:KFN10175.1, ECO:0000313|Proteomes:UP000029278};
RN [1] {ECO:0000313|EMBL:KFN10175.1, ECO:0000313|Proteomes:UP000029278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8244 {ECO:0000313|EMBL:KFN10175.1,
RC ECO:0000313|Proteomes:UP000029278};
RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA Scholz M.B., Teshima H., Xu Y.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MUG25519.1, ECO:0000313|Proteomes:UP000442469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3CT49 {ECO:0000313|EMBL:MUG25519.1,
RC ECO:0000313|Proteomes:UP000442469};
RA Olajide A.M., Chen S., Lapointe G.;
RT "Draft genome sequences of five Paenibacillus species of dairy origin.";
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFN10175.1}.
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DR EMBL; JMQA01000020; KFN10175.1; -; Genomic_DNA.
DR EMBL; WNZZ01000026; MUG25519.1; -; Genomic_DNA.
DR RefSeq; WP_036620989.1; NZ_WNZZ01000026.1.
DR AlphaFoldDB; A0A090ZIV4; -.
DR STRING; 44252.DJ90_440; -.
DR GeneID; 77012255; -.
DR PATRIC; fig|44252.3.peg.1677; -.
DR HOGENOM; CLU_039395_0_1_9; -.
DR OrthoDB; 9761504at2; -.
DR UniPathway; UPA00541; UER00602.
DR Proteomes; UP000029278; Unassembled WGS sequence.
DR Proteomes; UP000442469; Unassembled WGS sequence.
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; SUGAR KINASE; 1.
DR PANTHER; PTHR43095:SF5; XYLULOSE 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:KFN10175.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01535};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01535};
KW Reference proteome {ECO:0000313|Proteomes:UP000029278};
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:KFN10175.1}.
FT DOMAIN 5..242
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 252..439
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT ACT_SITE 235
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT BINDING 11..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT BINDING 234..236
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT BINDING 257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT BINDING 302
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT BINDING 401
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
FT DISULFID 352..369
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01535"
SQ SEQUENCE 489 AA; 54559 MW; EEAD73ECDBF1D6B1 CRC64;
MNHHIAVDIG ASSGRLVAGN LQDGLMTLRE IHRFDNGFAE KNGHFYWDID HLFREILRGL
TEAKRLGIEK CTLGIDTWAV DYALLDSQGE RIGDVFSYRD PRTNEAVDEV HRQMPFAKIY
AKTGIQHLSF NTLYQLYAHD RRELAAAEQI LLVPDYLYYL LSGRPIHEAT NASTTAMLNL
QTRDYDPELL ALLGLPRAKF PALTEPGTPL GPLKPELMQA YDLPECELIC AATHDTASAV
LGVPARGESW GYLSSGTWSL IGVERDAPLA TREAMERNYT NEWGAYGTYR FLKNIMGMWL
IQEVRKDYGK QYSFAELVTL AEEVPPFRSL ISCNDDRFLN PRHMTEEIRR YCAETGQPVP
DTPGEVARCI FDSLALSYDF YIKELERLTG EKINTLHIVG GGANNELLCQ LTADVLGIAV
EAGPTESTAL GNLAVQMVSC GVISNIGEAR EIIRRSFPVR SYAPQPVDPE AIAEARSRFA
ALTALTDHP
//
