ID PUR9_COLP3 Reviewed; 533 AA.
AC Q489F4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 102.
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=CPS_0552;
OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS psychroerythus).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=167879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=34H / ATCC BAA-681;
RX PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT "The psychrophilic lifestyle as revealed by the genome sequence of
RT Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-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:58467,
CC ChEBI:CHEBI:58475, ChEBI:CHEBI:195366; 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; CP000083; AAZ28762.1; -; Genomic_DNA.
DR RefSeq; WP_011041413.1; NC_003910.7.
DR AlphaFoldDB; Q489F4; -.
DR SMR; Q489F4; -.
DR STRING; 167879.CPS_0552; -.
DR KEGG; cps:CPS_0552; -.
DR eggNOG; COG0138; Bacteria.
DR HOGENOM; CLU_016316_5_2_6; -.
DR UniPathway; UPA00074; UER00133.
DR UniPathway; UPA00074; UER00135.
DR Proteomes; UP000000547; 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 CDD; cd01421; IMPCH; 1.
DR Gene3D; 3.40.140.20; -; 2.
DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 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 NCBIfam; TIGR00355; purH; 1.
DR PANTHER; PTHR11692:SF0; BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN ATIC; 1.
DR PANTHER; PTHR11692; BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN PURH; 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; SSF53927; Cytidine deaminase-like; 1.
DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW Hydrolase; Multifunctional enzyme; Purine biosynthesis; Transferase.
FT CHAIN 1..533
FT /note="Bifunctional purine biosynthesis protein PurH"
FT /id="PRO_1000018883"
FT DOMAIN 1..148
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
SQ SEQUENCE 533 AA; 57793 MW; 9D91E97F3A8FF883 CRC64;
MDTPRPIKRA LLSVSDKAGI VEFAQRLSEK GVDLLSTGGT AKLLAENGIK VTEVSDYTGH
PEIMDGRVKT LHPKVHGGIL ARRGIDEVVM DENGISAIDM VVVNLYPFAN AVSDENCSLE
NAIENIDIGG PTMVRAAAKN HKDVTIVVNA SDYERVLTEL DNNNDSLTYK TRFDLAIAAY
EHTASYDGMI ANYFGKMLPA YGETESKASL ENKVKFPRTF NSQFIKTQDL RYGENSHQDA
AFYKEENPEE ASVSTATQLQ GKALSYNNIA DTDAALECVK EFDEPACVIV KHANPCGVAI
GDDILAAYEG AYKTDPTSAF GGIIAFNREL DADTAEAIVS RQFVEVIIAP SVSDAAAQIV
AAKPNLRLLE CGQWDNKTTG FDFKRVNGGL LVQDTDQGRV TSDDLTVVTK RQPTDEEMRD
LQFCWKVAKF VKSNAIVYVK NSSTIGVGAG QMSRVYSAKV AGIKAADENL EVKGSVMASD
AFFPFRDGLD AAAEAGITAV IQPGGSMRDD EVIAAADEHN IAMVFTGMRH FRH
//
