PUR9_MYCPA
ID PUR9_MYCPA Reviewed; 527 AA.
AC Q9RAJ5;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 25-MAY-2022, entry version 115.
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=MAP_0903;
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 19698 / CIP 103963 / DSM 44133 / TMC 807;
RA Urbanic K.U., Raymond M., Mutharia L.M.;
RT "Identification of the purine biosynthetic genes purN and purH in
RT Mycobacterium avium subsp. paratuberculosis.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10;
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS03220.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF191543; AAF05727.1; -; Genomic_DNA.
DR EMBL; AE016958; AAS03220.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_040963270.1; NC_002944.2.
DR AlphaFoldDB; Q9RAJ5; -.
DR SMR; Q9RAJ5; -.
DR STRING; 262316.MAP_0903; -.
DR PRIDE; Q9RAJ5; -.
DR EnsemblBacteria; AAS03220; AAS03220; MAP_0903.
DR KEGG; mpa:MAP_0903; -.
DR PATRIC; fig|262316.17.peg.944; -.
DR eggNOG; COG0138; Bacteria.
DR HOGENOM; CLU_016316_5_2_11; -.
DR OMA; WRVAKFV; -.
DR UniPathway; UPA00074; UER00133.
DR UniPathway; UPA00074; UER00135.
DR Proteomes; UP000000580; 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..527
FT /note="Bifunctional purine biosynthesis protein PurH"
FT /id="PRO_0000192105"
FT DOMAIN 9..156
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT CONFLICT 63
FT /note="V -> E (in Ref. 1; AAF05727)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="A -> V (in Ref. 1; AAF05727)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="A -> V (in Ref. 1; AAF05727)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 527 AA; 55888 MW; 8B4459CFB40EC338 CRC64;
MSTDDWRENA KRPIRRALIS VYDKTGLVEL AQGLTEAGVE IVSTGSTAKV IAEKGIPVTR
VEVLTGFPEV LDGRVKTLHP RVHAGLLADL RKPEHAAALE QLGIAAFELV VVNLYPFTET
VDSGAGIDEC VEQIDIGGPS MVRAAAKNHP SVAVVVDPLG YDGVLAAVRH GGFTLAERKR
LAALAFQHTA DYDIAVATWM ESTLAPEHPP TTFPKWLGRS WRRSAMLRYG ENPHQQASLY
SDPGAWPGLA QAEQLHGKEM SYNNFTDADA AWRAAFDHEQ TCVAIIKHAN PCGIAISSIS
VADAHRKAHE CDPLSAFGGV IAANTEVSVE MAEYVSTIFT EVIIAPAYQP AALEILTRKK
NIRVLVASEP LTGGTELRPI SGGLLVQQRD ELDAHGDNPA NWTLATGAPA DPATLADLVF
AWRVCRAVKS NAIVIAAGGA TIGVGMGQVN RVDAARLAVE RGGDRVRGAV AASDAFFPFP
DGLETLTGAG VKAVVHPGGS VRDDEVTAAA ANAGITLYLT GARHFAH
