PUR9_CAMJE
ID PUR9_CAMJE Reviewed; 510 AA.
AC Q9PNY2; Q0P9U6;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=Cj0953c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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; AL111168; CAL35073.1; -; Genomic_DNA.
DR PIR; H81369; H81369.
DR RefSeq; WP_002853339.1; NC_002163.1.
DR RefSeq; YP_002344351.1; NC_002163.1.
DR PDB; 4EHI; X-ray; 2.28 A; A/B=1-510.
DR PDBsum; 4EHI; -.
DR AlphaFoldDB; Q9PNY2; -.
DR SMR; Q9PNY2; -.
DR IntAct; Q9PNY2; 1.
DR STRING; 192222.Cj0953c; -.
DR PaxDb; Q9PNY2; -.
DR PRIDE; Q9PNY2; -.
DR EnsemblBacteria; CAL35073; CAL35073; Cj0953c.
DR GeneID; 905247; -.
DR KEGG; cje:Cj0953c; -.
DR PATRIC; fig|192222.6.peg.937; -.
DR eggNOG; COG0138; Bacteria.
DR HOGENOM; CLU_016316_5_2_7; -.
DR OMA; WRVAKFV; -.
DR UniPathway; UPA00074; UER00133.
DR UniPathway; UPA00074; UER00135.
DR Proteomes; UP000000799; 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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Multifunctional enzyme; Purine biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..510
FT /note="Bifunctional purine biosynthesis protein PurH"
FT /id="PRO_0000192079"
FT DOMAIN 1..142
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:4EHI"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:4EHI"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:4EHI"
FT HELIX 31..39
FT /evidence="ECO:0007829|PDB:4EHI"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:4EHI"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:4EHI"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:4EHI"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:4EHI"
FT HELIX 113..118
FT /evidence="ECO:0007829|PDB:4EHI"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:4EHI"
FT TURN 134..137
FT /evidence="ECO:0007829|PDB:4EHI"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:4EHI"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:4EHI"
FT HELIX 147..155
FT /evidence="ECO:0007829|PDB:4EHI"
FT HELIX 161..190
FT /evidence="ECO:0007829|PDB:4EHI"
FT STRAND 196..209
FT /evidence="ECO:0007829|PDB:4EHI"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:4EHI"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:4EHI"
FT HELIX 226..230
FT /evidence="ECO:0007829|PDB:4EHI"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:4EHI"
FT HELIX 240..253
FT /evidence="ECO:0007829|PDB:4EHI"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:4EHI"
FT STRAND 269..275
FT /evidence="ECO:0007829|PDB:4EHI"
FT HELIX 279..287
FT /evidence="ECO:0007829|PDB:4EHI"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:4EHI"
FT STRAND 298..305
FT /evidence="ECO:0007829|PDB:4EHI"
FT HELIX 307..313
FT /evidence="ECO:0007829|PDB:4EHI"
FT STRAND 319..326
FT /evidence="ECO:0007829|PDB:4EHI"
FT HELIX 328..332
FT /evidence="ECO:0007829|PDB:4EHI"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:4EHI"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:4EHI"
FT STRAND 356..362
FT /evidence="ECO:0007829|PDB:4EHI"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:4EHI"
FT TURN 376..381
FT /evidence="ECO:0007829|PDB:4EHI"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:4EHI"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:4EHI"
FT HELIX 392..407
FT /evidence="ECO:0007829|PDB:4EHI"
FT STRAND 413..417
FT /evidence="ECO:0007829|PDB:4EHI"
FT STRAND 420..425
FT /evidence="ECO:0007829|PDB:4EHI"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:4EHI"
FT HELIX 431..444
FT /evidence="ECO:0007829|PDB:4EHI"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:4EHI"
FT HELIX 464..471
FT /evidence="ECO:0007829|PDB:4EHI"
FT STRAND 476..479
FT /evidence="ECO:0007829|PDB:4EHI"
FT HELIX 486..496
FT /evidence="ECO:0007829|PDB:4EHI"
FT STRAND 499..502
FT /evidence="ECO:0007829|PDB:4EHI"
SQ SEQUENCE 510 AA; 56402 MW; 56F356F04B3A2092 CRC64;
MRALLSVSDK EGIVEFGKEL ENLGFEILST GGTFKLLKEN GIKVIEVSDF TKSPELFEGR
VKTLHPKIHG GILHKRSDEN HIKQAKENEI LGIDLVCVNL YPFKKTTIMS DDFDEIIENI
DIGGPAMIRS AAKNYKDVMV LCDPLDYEKV IETLKKGQND ENFRLNLMIK AYEHTANYDA
YIANYMNERF NGGFGASKFI VGQKVFDTKY GENPHQKGAL YEFDAFFSAN FKALKGEASF
NNLTDINAAL NLASSFDKAP AIAIVKHGNP CGFAIKENLV QSYIHALKCD SVSAYGGVVA
INGTLDEALA NKINEIYVEV IIAANVDEKA LAVFEGKKRI KIFTQESPFL IRSFDKYDFK
HIDGGFVYQN SDEVGEDELK NAKLMSQREA SKEELKDLEI AMKIAAFTKS NNVVYVKNGA
MVAIGMGMTS RIDAAKAAIA KAKEMGLDLQ GCVLASEAFF PFRDSIDEAS KVGVKAIVEP
GGSIRDDEVV KAADEYGMAL YFTGVRHFLH
