PUR9_STRCO
ID PUR9_STRCO Reviewed; 523 AA.
AC Q9KY50;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Bifunctional purine biosynthesis protein PurH {ECO:0000255|HAMAP-Rule:MF_00139};
DE Includes:
DE RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase {ECO:0000255|HAMAP-Rule:MF_00139};
DE EC=2.1.2.3 {ECO:0000255|HAMAP-Rule:MF_00139};
DE AltName: Full=AICAR transformylase {ECO:0000255|HAMAP-Rule:MF_00139};
DE Includes:
DE RecName: Full=IMP cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_00139};
DE EC=3.5.4.10 {ECO:0000255|HAMAP-Rule:MF_00139};
DE AltName: Full=ATIC {ECO:0000255|HAMAP-Rule:MF_00139};
DE AltName: Full=IMP synthase {ECO:0000255|HAMAP-Rule:MF_00139};
DE AltName: Full=Inosinicase {ECO:0000255|HAMAP-Rule:MF_00139};
GN Name=purH {ECO:0000255|HAMAP-Rule:MF_00139}; OrderedLocusNames=SCO4814;
GN ORFNames=SCD63A.25;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-
CC ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-
CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide;
CC Xref=Rhea:RHEA:22192, ChEBI:CHEBI:57453, ChEBI:CHEBI:57454,
CC ChEBI:CHEBI:58467, ChEBI:CHEBI:58475; EC=2.1.2.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00139};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-
CC carboxamide; Xref=Rhea:RHEA:18445, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:58467; EC=3.5.4.10;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00139};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-
CC 1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route):
CC step 1/1. {ECO:0000255|HAMAP-Rule:MF_00139}.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; IMP
CC from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step
CC 1/1. {ECO:0000255|HAMAP-Rule:MF_00139}.
CC -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal
CC region. {ECO:0000255|HAMAP-Rule:MF_00139}.
CC -!- SIMILARITY: Belongs to the PurH family. {ECO:0000255|HAMAP-
CC Rule:MF_00139}.
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DR EMBL; AL939121; CAB92677.1; -; Genomic_DNA.
DR RefSeq; NP_628971.1; NC_003888.3.
DR RefSeq; WP_011029883.1; NZ_VNID01000016.1.
DR AlphaFoldDB; Q9KY50; -.
DR SMR; Q9KY50; -.
DR STRING; 100226.SCO4814; -.
DR GeneID; 1100255; -.
DR KEGG; sco:SCO4814; -.
DR PATRIC; fig|100226.15.peg.4891; -.
DR eggNOG; COG0138; Bacteria.
DR HOGENOM; CLU_016316_5_2_11; -.
DR InParanoid; Q9KY50; -.
DR OMA; WRVAKFV; -.
DR PhylomeDB; Q9KY50; -.
DR UniPathway; UPA00074; UER00133.
DR UniPathway; UPA00074; UER00135.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003937; F:IMP cyclohydrolase activity; IBA:GO_Central.
DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IBA:GO_Central.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.140.20; -; 2.
DR Gene3D; 3.40.50.1380; -; 1.
DR HAMAP; MF_00139; PurH; 1.
DR InterPro; IPR024051; AICAR_Tfase_dup_dom_sf.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR002695; PurH-like.
DR PANTHER; PTHR11692; PTHR11692; 1.
DR Pfam; PF01808; AICARFT_IMPCHas; 1.
DR Pfam; PF02142; MGS; 1.
DR PIRSF; PIRSF000414; AICARFT_IMPCHas; 1.
DR SMART; SM00798; AICARFT_IMPCHas; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF52335; SSF52335; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR TIGRFAMs; TIGR00355; purH; 1.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW Hydrolase; Multifunctional enzyme; Purine biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..523
FT /note="Bifunctional purine biosynthesis protein PurH"
FT /id="PRO_0000192132"
FT DOMAIN 1..154
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
SQ SEQUENCE 523 AA; 55043 MW; 10A16ADA490E350F CRC64;
MTATAGSNKR AIRRALVSVY DKTGLEDLAR GLHEAGVELV STGSTAGRIA AAGVPVTKVE
ELTGFPECLD GRVKTLHPKV HAGILADLRL ESHRQQLDEL GVAPFDLVVV NLYPFRETVA
SGATPDECVE QIDIGGPSMV RAAAKNHPSV AVVTSPARYA DVLLAVEGGG FDLAARKRLA
AEAFQHTAAY DVAVASWFAA EYAPVDESGF PDFLGATYER ANTLRYGENP HQPAALYTSP
EGGGLAQAEQ LHGKEMSYNN YTDTDAARRA AYDHAEPCVA IIKHANPCGI AIGADVAEAH
RKAHDCDPVS AYGGVIAVNR PVSKEMAERV AGIFTEVIVA PDYEDGALEA LTKKKNIRVL
RAPAAPAAPV EVKPIDGGAL LQVTDRLQAE GDDPATWTLA TGEALSEAEL AELAFAWRAC
RAVKSNAILL AKDGASVGVG MGQVNRVDSA KLAVERAGAE RAQGAYAASD AFFPFPDGLE
ILTGAGVKAV VQPGGSVRDE LVVEAAKKAG VTMYFTGTRH FFH
