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Database: UniProt
Entry: N1V2H0_9MICC
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Original site: N1V2H0_9MICC 
ID   N1V2H0_9MICC            Unreviewed;       574 AA.
AC   N1V2H0;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Ribulokinase {ECO:0000256|HAMAP-Rule:MF_00520, ECO:0000256|RuleBase:RU003455};
DE            EC=2.7.1.16 {ECO:0000256|HAMAP-Rule:MF_00520, ECO:0000256|RuleBase:RU003455};
GN   Name=araB {ECO:0000256|HAMAP-Rule:MF_00520};
GN   ORFNames=D477_003853 {ECO:0000313|EMBL:EMY35545.1};
OS   Arthrobacter crystallopoietes BAB-32.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1246476 {ECO:0000313|EMBL:EMY35545.1, ECO:0000313|Proteomes:UP000010729};
RN   [1] {ECO:0000313|EMBL:EMY35545.1, ECO:0000313|Proteomes:UP000010729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAB-32 {ECO:0000313|EMBL:EMY35545.1,
RC   ECO:0000313|Proteomes:UP000010729};
RX   PubMed=23833141;
RA   Joshi M.N., Pandit A.S., Sharma A., Pandya R.V., Desai S.M., Saxena A.K.,
RA   Bagatharia S.B.;
RT   "Draft Genome Sequence of Arthrobacter crystallopoietes Strain BAB-32,
RT   Revealing Genes for Bioremediation.";
RL   Genome Announc. 1:e00452-13(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-ribulose = ADP + D-ribulose 5-phosphate + H(+);
CC         Xref=Rhea:RHEA:17601, ChEBI:CHEBI:15378, ChEBI:CHEBI:17173,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58121, ChEBI:CHEBI:456216;
CC         EC=2.7.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00520};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-ribulose = ADP + H(+) + L-ribulose 5-phosphate;
CC         Xref=Rhea:RHEA:22072, ChEBI:CHEBI:15378, ChEBI:CHEBI:16880,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58226, ChEBI:CHEBI:456216;
CC         EC=2.7.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00520,
CC         ECO:0000256|RuleBase:RU003455};
CC   -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC       ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route):
CC       step 2/3. {ECO:0000256|HAMAP-Rule:MF_00520,
CC       ECO:0000256|RuleBase:RU003455}.
CC   -!- SIMILARITY: Belongs to the ribulokinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00520, ECO:0000256|RuleBase:RU003455}.
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:EMY35545.1}.
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DR   EMBL; ANPE02000070; EMY35545.1; -; Genomic_DNA.
DR   RefSeq; WP_005267417.1; NZ_ANPE02000070.1.
DR   AlphaFoldDB; N1V2H0; -.
DR   OrthoDB; 9805576at2; -.
DR   UniPathway; UPA00145; UER00566.
DR   Proteomes; UP000010729; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019150; F:D-ribulokinase activity; IEA:RHEA.
DR   GO; GO:0008741; F:ribulokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IEA:UniProtKB-UniRule.
DR   CDD; cd07781; FGGY_RBK; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_00520; Ribulokinase; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
DR   InterPro; IPR018485; FGGY_C.
DR   InterPro; IPR018484; FGGY_N.
DR   InterPro; IPR005929; Ribulokinase.
DR   NCBIfam; TIGR01234; L-ribulokinase; 1.
DR   PANTHER; PTHR43435:SF4; FGGY CARBOHYDRATE KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43435; RIBULOKINASE; 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   Arabinose catabolism {ECO:0000256|ARBA:ARBA00022935, ECO:0000256|HAMAP-
KW   Rule:MF_00520}; ATP-binding {ECO:0000256|HAMAP-Rule:MF_00520};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_00520};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00520, ECO:0000256|RuleBase:RU003455};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00520};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010729};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00520,
KW   ECO:0000256|RuleBase:RU003455}.
FT   DOMAIN          9..285
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          298..495
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
SQ   SEQUENCE   574 AA;  61561 MW;  325066E0619713F8 CRC64;
     MSHPKENEYV IGVDFGTLSG RALVVRVSDG REMGSAVHPY PHAVITSALT SDLTGNEPVR
     LPVDWALQVP QDYREVLQQA VPQAIAAAGI VPDTVVGIAV DFTACTMIPT LNDGTPLCEV
     DGLLAEPHAY AKLWRHHAAQ AQADRINELA CSRNEPWLAR YGGLISSEWE FAKALQLLEE
     APQVYAQLER WVEAADWIVW ELCGEYVRNA CTAGYKGMLQ DGHYPSSDFC AELNPDFATF
     VEDKLDQPIG QLAGRAGTLT SEAAEWTGLR EGIAVAVGNV DAHVTAPAAR AVAPGQMVAI
     MGTSTCHVMN GAAVLEVPGM CGAVEGGIVS GLWGYEAGQS GVGDIFAWFV ENIVPRSYYD
     AAESAGLTIH EHLTELAKDQ EVGQHGLIAL DWHSGNRSVL VDHELSSVIV GQTLATRPED
     VYRALLEATA FGARTIVEAF NNSDVPVKEF IAAGGLIRNS FLMQVYADIL NMPVRTIGST
     QGPALGSAIH AAVAAGAYPD IHAASEAMGA AAGIVYEPIP YNVARYEELF AEYTALHDYF
     GRGANTVMHR LKRFQRNAME RAAQPVGAGI ILTN
//
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