ID Q4FSN2_PSYA2 Unreviewed; 187 AA.
AC Q4FSN2;
DT 30-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=Probable hypoxanthine/xanthine/guanine phosphoribosyltransferase {ECO:0000313|EMBL:AAZ18976.1};
DE EC=2.4.2.8 {ECO:0000313|EMBL:AAZ18976.1};
GN Name=hpt {ECO:0000313|EMBL:AAZ18976.1};
GN OrderedLocusNames=Psyc_1125 {ECO:0000313|EMBL:AAZ18976.1};
OS Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=259536 {ECO:0000313|EMBL:AAZ18976.1, ECO:0000313|Proteomes:UP000000546};
RN [1] {ECO:0000313|EMBL:AAZ18976.1, ECO:0000313|Proteomes:UP000000546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17307 / VKM B-2377 / 273-4
RC {ECO:0000313|Proteomes:UP000000546};
RX PubMed=20154119; DOI=10.1128/AEM.02101-09;
RA Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA Murray A., Thomashow M., Tiedje J.M.;
RT "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT temperature growth.";
RL Appl. Environ. Microbiol. 76:2304-2312(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + GMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC guanine; Xref=Rhea:RHEA:25424, ChEBI:CHEBI:16235, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58017, ChEBI:CHEBI:58115; EC=2.4.2.8;
CC Evidence={ECO:0000256|ARBA:ARBA00000210};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25426;
CC Evidence={ECO:0000256|ARBA:ARBA00000210};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate +
CC hypoxanthine; Xref=Rhea:RHEA:17973, ChEBI:CHEBI:17368,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58053; EC=2.4.2.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001442};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17975;
CC Evidence={ECO:0000256|ARBA:ARBA00001442};
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DR EMBL; CP000082; AAZ18976.1; -; Genomic_DNA.
DR RefSeq; WP_011280398.1; NC_007204.1.
DR AlphaFoldDB; Q4FSN2; -.
DR STRING; 259536.Psyc_1125; -.
DR KEGG; par:Psyc_1125; -.
DR eggNOG; COG0634; Bacteria.
DR HOGENOM; CLU_073615_2_0_6; -.
DR OrthoDB; 9802824at2; -.
DR Proteomes; UP000000546; Chromosome.
DR GO; GO:0052657; F:guanine phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR PANTHER; PTHR43340:SF1; HYPOXANTHINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR43340; HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000313|EMBL:AAZ18976.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000546};
KW Transferase {ECO:0000313|EMBL:AAZ18976.1}.
FT DOMAIN 26..154
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
SQ SEQUENCE 187 AA; 21275 MW; 504445BA42124BE0 CRC64;
MTQISNQEIE KTLRNSECLI SSIEVAAAYE RLAAQLNLHY AGLNPIVMVV MNGGLIPAGQ
LLTHLTFYHR MHYIHASRYR DNEGTNELDW KFKPDVSIAG EYVLLIDDIF DEGITLKSIV
EELSKENPLS IESCVLLNKE HDRKVVDFDV DFVGINVADR YVYGCGMDFH GYLRHLPGIY
AIKEDKI
//
