ID G9Y8Q5_HAFAL Unreviewed; 187 AA.
AC G9Y8Q5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Ribose 1,5-bisphosphate phosphokinase PhnN {ECO:0000256|HAMAP-Rule:MF_00836};
DE EC=2.7.4.23 {ECO:0000256|HAMAP-Rule:MF_00836};
DE AltName: Full=Ribose 1,5-bisphosphokinase {ECO:0000256|HAMAP-Rule:MF_00836};
GN Name=phnN {ECO:0000256|HAMAP-Rule:MF_00836};
GN ORFNames=HMPREF0454_03048 {ECO:0000313|EMBL:EHM41286.1};
OS Hafnia alvei ATCC 51873.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Hafnia.
OX NCBI_TaxID=1002364 {ECO:0000313|EMBL:EHM41286.1, ECO:0000313|Proteomes:UP000005959};
RN [1] {ECO:0000313|EMBL:EHM41286.1, ECO:0000313|Proteomes:UP000005959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51873 {ECO:0000313|EMBL:EHM41286.1,
RC ECO:0000313|Proteomes:UP000005959};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of ribose 1,5-bisphosphate to
CC 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP). {ECO:0000256|HAMAP-
CC Rule:MF_00836}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-ribose 1,5-bisphosphate + ATP = 5-phospho-alpha-D-
CC ribose 1-diphosphate + ADP; Xref=Rhea:RHEA:20109, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58017, ChEBI:CHEBI:68688, ChEBI:CHEBI:456216;
CC EC=2.7.4.23; Evidence={ECO:0000256|ARBA:ARBA00000373,
CC ECO:0000256|HAMAP-Rule:MF_00836};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose
CC 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from
CC D-ribose 5-phosphate (route II): step 3/3.
CC {ECO:0000256|ARBA:ARBA00005069, ECO:0000256|HAMAP-Rule:MF_00836}.
CC -!- SIMILARITY: Belongs to the ribose 1,5-bisphosphokinase family.
CC {ECO:0000256|HAMAP-Rule:MF_00836}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00836}.
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:EHM41286.1}.
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DR EMBL; AGCI01000069; EHM41286.1; -; Genomic_DNA.
DR RefSeq; WP_004093766.1; NZ_JH417532.1.
DR AlphaFoldDB; G9Y8Q5; -.
DR PATRIC; fig|1002364.3.peg.2756; -.
DR HOGENOM; CLU_102477_0_0_6; -.
DR UniPathway; UPA00087; UER00175.
DR Proteomes; UP000005959; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0033863; F:ribose 1,5-bisphosphate phosphokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019634; P:organic phosphonate metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00836; PhnN; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012699; PhnN.
DR NCBIfam; TIGR02322; phosphon_PhnN; 1.
DR PANTHER; PTHR23117; GUANYLATE KINASE-RELATED; 1.
DR PANTHER; PTHR23117:SF8; RIBOSE 1,5-BISPHOSPHATE PHOSPHOKINASE PHNN; 1.
DR Pfam; PF13238; AAA_18; 1.
DR SMART; SM00072; GuKc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00836};
KW Kinase {ECO:0000313|EMBL:EHM41286.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00836};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00836}.
FT DOMAIN 1..181
FT /note="Guanylate kinase/L-type calcium channel beta
FT subunit"
FT /evidence="ECO:0000259|SMART:SM00072"
SQ SEQUENCE 187 AA; 21026 MW; 46160D428D9854F4 CRC64;
MGKLIYLVGA SGSGKDSLLQ ALREQQTIPL LVAHRYITRA CNAGSENHIE LSETEFMQRR
SQGLFALNWQ ANQHYYALGI EIDQWLAQGI NVVVNGSRAH LPVARERYGN AMLAVCLQVS
PDILRQRLQA RGRETPQQIE QRLQRARDYQ LAENTGCYYL NNNDGLSHTV QAFLRLMAET
TPVSVSA
//
