PUR9_LACDA
ID PUR9_LACDA Reviewed; 513 AA.
AC Q1G9G2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=Ldb1436;
OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS 00102 / Lb 14).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=390333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB
RC 11778 / NCTC 12712 / WDCM 00102 / Lb 14;
RX PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA Weissenbach J., Ehrlich S.D., Maguin E.;
RT "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT and ongoing reductive evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
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; CR954253; CAI98237.1; -; Genomic_DNA.
DR RefSeq; WP_003618422.1; NZ_JQAV01000009.1.
DR AlphaFoldDB; Q1G9G2; -.
DR SMR; Q1G9G2; -.
DR STRING; 390333.Ldb1436; -.
DR EnsemblBacteria; CAI98237; CAI98237; Ldb1436.
DR KEGG; ldb:Ldb1436; -.
DR PATRIC; fig|390333.13.peg.1932; -.
DR eggNOG; COG0138; Bacteria.
DR HOGENOM; CLU_016316_5_2_9; -.
DR OMA; WRVAKFV; -.
DR BioCyc; LDEL390333:LDB_RS06180-MON; -.
DR UniPathway; UPA00074; UER00133.
DR UniPathway; UPA00074; UER00135.
DR Proteomes; UP000001259; Chromosome.
DR GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
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..513
FT /note="Bifunctional purine biosynthesis protein PurH"
FT /id="PRO_1000018898"
FT DOMAIN 1..144
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
SQ SEQUENCE 513 AA; 56628 MW; 275DF1135A5B8703 CRC64;
MKRALVSVSD KNNLVPFVKG LVANDYEIVS TGGTKRVLDE AGIPTISVED VTGFPEILDG
RVKTLNPYIH GGLLARRELP EHVATLKEHK ITPIDLVCVN LYPFKQTIEK PDVTLAEAIE
NIDIGGPSMV RSASKNYRDV TIVVDQADYD QVLAEIEKDG STSLETRARL AAKAFRLTAS
YDALISQYLT EKAGETAPEK LTLTYDLKEA MRYGENSHQK AWLYEDALPK AFSVLQAEQL
NGKELSYNNI KDADEALRCV REFSKPTVVA MKHMNPCGIG QGNTLEEAWD RAYVADPVSI
FGGVIALNRK VDLATAEKMH KIFLEIIIAP DYDEDALAAL KTKKKNLRIL KLDFSKKDEA
TSKETVSVMG GLLVQDQDVL DEDFADWECV TEAKPTQEQL ESLLFAWKAV KHTKSNAIVV
ANNERTLGVG AGQPNRIDSE KIAIDHAAEA LDDRAVLASD AFFPFSDCVE YAGKHGIKAI
VQPGGSVRDQ ESIDMANKYG IAMVFTGVRH FRH
