LOGH_PSEAE
ID LOGH_PSEAE Reviewed; 195 AA.
AC P48636; Q9HUP1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase {ECO:0000250|UniProtKB:O05306};
DE EC=3.2.2.n1 {ECO:0000250|UniProtKB:O05306};
DE AltName: Full=AMP nucleosidase {ECO:0000305};
DE EC=3.2.2.4 {ECO:0000269|PubMed:29901273};
DE AltName: Full=PaLOG {ECO:0000303|PubMed:29901273};
GN OrderedLocusNames=PA4923;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71.
RX PubMed=2116366; DOI=10.1016/0378-1119(90)90434-s;
RA Hoitink C.W.G., Woudt L.P., Turenhout J.C.M., van de Kamp M., Canters G.W.;
RT "Isolation and sequencing of the Alcaligenes denitrificans azurin-encoding
RT gene: comparison with the genes encoding blue copper proteins from
RT Pseudomonas aeruginosa and Alcaligenes faecalis.";
RL Gene 90:15-20(1990).
RN [3] {ECO:0007744|PDB:5ZBJ, ECO:0007744|PDB:5ZBK}
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP AMP, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, AND MUTAGENESIS OF
RP MET-89; ARG-92; THR-112; GLU-114; GLU-115 AND GLU-118.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=29901273; DOI=10.1111/1462-2920.14287;
RA Seo H., Kim K.J.;
RT "Structural insight into molecular mechanism of cytokinin activating
RT protein from Pseudomonas aeruginosa PAO1.";
RL Environ. Microbiol. 20:3214-3223(2018).
CC -!- FUNCTION: Catalyzes the hydrolytic removal of ribose 5'-monophosphate
CC from nitrogen N6-modified adenosines, the final step of bioactive
CC cytokinin synthesis (Probable). Exhibits phosphoribohydrolase activity
CC against AMP in vitro (PubMed:29901273). {ECO:0000269|PubMed:29901273,
CC ECO:0000305|PubMed:29901273}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-(dimethylallyl)adenosine 5'-phosphate = D-ribose 5-
CC phosphate + N(6)-dimethylallyladenine; Xref=Rhea:RHEA:48560,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17660, ChEBI:CHEBI:57526,
CC ChEBI:CHEBI:78346; EC=3.2.2.n1;
CC Evidence={ECO:0000250|UniProtKB:O05306};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-ribosyl-trans-zeatin 5'-phosphate + H2O = D-ribose 5-
CC phosphate + trans-zeatin; Xref=Rhea:RHEA:48564, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16522, ChEBI:CHEBI:78346, ChEBI:CHEBI:87947; EC=3.2.2.n1;
CC Evidence={ECO:0000250|UniProtKB:O05306};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + H2O = adenine + D-ribose 5-phosphate;
CC Xref=Rhea:RHEA:20129, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708,
CC ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=3.2.2.4;
CC Evidence={ECO:0000269|PubMed:29901273};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:29901273}.
CC -!- DOMAIN: Undergoes an open/closed conformational change upon binding
CC AMP. {ECO:0000269|PubMed:29901273}.
CC -!- SIMILARITY: Belongs to the LOG family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG08308.1; -; Genomic_DNA.
DR EMBL; M30389; AAA25729.2; -; Genomic_DNA.
DR PIR; A83031; A83031.
DR PIR; PQ0114; PQ0114.
DR RefSeq; NP_253610.1; NC_002516.2.
DR RefSeq; WP_003109460.1; NZ_QZGE01000002.1.
DR PDB; 5ZBJ; X-ray; 1.89 A; A=1-195.
DR PDB; 5ZBK; X-ray; 2.30 A; A=1-195.
DR PDBsum; 5ZBJ; -.
DR PDBsum; 5ZBK; -.
DR AlphaFoldDB; P48636; -.
DR SMR; P48636; -.
DR STRING; 287.DR97_2274; -.
DR PaxDb; P48636; -.
DR PRIDE; P48636; -.
DR DNASU; 879697; -.
DR EnsemblBacteria; AAG08308; AAG08308; PA4923.
DR GeneID; 879697; -.
DR KEGG; pae:PA4923; -.
DR PATRIC; fig|208964.12.peg.5156; -.
DR PseudoCAP; PA4923; -.
DR HOGENOM; CLU_058336_4_2_6; -.
DR InParanoid; P48636; -.
DR OMA; HQKPIGL; -.
DR PhylomeDB; P48636; -.
DR BioCyc; PAER208964:G1FZ6-5037-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008714; F:AMP nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0016799; F:hydrolase activity, hydrolyzing N-glycosyl compounds; IDA:PseudoCAP.
DR GO; GO:0102682; F:N6-(Delta2-isopentenyl)-adenosine 5'-monophosphate phosphoribohydrolase activity; IEA:RHEA.
DR GO; GO:0009691; P:cytokinin biosynthetic process; IBA:GO_Central.
DR InterPro; IPR005269; LOG.
DR InterPro; IPR031100; LOG_fam.
DR Pfam; PF03641; Lysine_decarbox; 1.
DR TIGRFAMs; TIGR00730; TIGR00730; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytokinin biosynthesis; Hydrolase; Reference proteome.
FT CHAIN 1..195
FT /note="Cytokinin riboside 5'-monophosphate
FT phosphoribohydrolase"
FT /id="PRO_0000206257"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29901273"
FT BINDING 92..93
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29901273"
FT BINDING 109..115
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29901273"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B2HS63"
FT MUTAGEN 89
FT /note="M->A: Almost complete loss of activity."
FT /evidence="ECO:0000269|PubMed:29901273"
FT MUTAGEN 92
FT /note="R->A: Almost complete loss of activity."
FT /evidence="ECO:0000269|PubMed:29901273"
FT MUTAGEN 112
FT /note="T->A: Almost complete loss of activity."
FT /evidence="ECO:0000269|PubMed:29901273"
FT MUTAGEN 114
FT /note="E->A: Almost complete loss of activity."
FT /evidence="ECO:0000269|PubMed:29901273"
FT MUTAGEN 115
FT /note="E->A: Almost complete loss of activity."
FT /evidence="ECO:0000269|PubMed:29901273"
FT MUTAGEN 118
FT /note="E->A: Retains 8% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:29901273"
FT CONFLICT 60
FT /note="G -> S (in Ref. 2; AAA25729)"
FT /evidence="ECO:0000305"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:5ZBJ"
FT HELIX 19..33
FT /evidence="ECO:0007829|PDB:5ZBJ"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:5ZBJ"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:5ZBJ"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:5ZBJ"
FT HELIX 68..72
FT /evidence="ECO:0007829|PDB:5ZBJ"
FT STRAND 78..88
FT /evidence="ECO:0007829|PDB:5ZBJ"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:5ZBJ"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:5ZBJ"
FT HELIX 110..124
FT /evidence="ECO:0007829|PDB:5ZBJ"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:5ZBJ"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:5ZBJ"
FT HELIX 142..153
FT /evidence="ECO:0007829|PDB:5ZBJ"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:5ZBJ"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:5ZBJ"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:5ZBJ"
SQ SEQUENCE 195 AA; 20725 MW; A5784C919D80361C CRC64;
MTLRSVCVFC GASPGASPVY QEAAVALGRH LAERGLTLVY GGGAVGLMGT VADAALAAGG
EVIGIIPQSL QEAEIGHKGL TRLEVVDGMH ARKARMAELA DAFIALPGGL GTLEELFEVW
TWGQLGYHAK PLGLLEVNGF YDPLLTFLDH LVDERFVRAE HRGMLQRGAS PEALLDALAA
WTPSVAPKWV DRTPQ
