PUR5_VIBCH
ID PUR5_VIBCH Reviewed; 346 AA.
AC Q9KPY6;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000255|HAMAP-Rule:MF_00741};
DE EC=6.3.3.1 {ECO:0000255|HAMAP-Rule:MF_00741};
DE AltName: Full=AIR synthase {ECO:0000255|HAMAP-Rule:MF_00741};
DE AltName: Full=AIRS {ECO:0000255|HAMAP-Rule:MF_00741};
DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase {ECO:0000255|HAMAP-Rule:MF_00741};
GN Name=purM {ECO:0000255|HAMAP-Rule:MF_00741}; OrderedLocusNames=VC_2226;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP
CC = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:137981,
CC ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.3.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00741};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC phospho-D-ribosyl)glycinamide: step 2/2. {ECO:0000255|HAMAP-
CC Rule:MF_00741}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00741}.
CC -!- SIMILARITY: Belongs to the AIR synthase family. {ECO:0000255|HAMAP-
CC Rule:MF_00741}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE003852; AAF95370.1; -; Genomic_DNA.
DR PIR; F82103; F82103.
DR RefSeq; NP_231857.1; NC_002505.1.
DR RefSeq; WP_000016423.1; NZ_LT906614.1.
DR PDB; 3P4E; X-ray; 1.77 A; A=1-346.
DR PDBsum; 3P4E; -.
DR AlphaFoldDB; Q9KPY6; -.
DR SMR; Q9KPY6; -.
DR STRING; 243277.VC_2226; -.
DR DNASU; 2613266; -.
DR EnsemblBacteria; AAF95370; AAF95370; VC_2226.
DR GeneID; 57740851; -.
DR KEGG; vch:VC_2226; -.
DR PATRIC; fig|243277.26.peg.2124; -.
DR eggNOG; COG0150; Bacteria.
DR HOGENOM; CLU_047116_0_0_6; -.
DR OMA; EPLFMTD; -.
DR BioCyc; VCHO:VC2226-MON; -.
DR UniPathway; UPA00074; UER00129.
DR EvolutionaryTrace; Q9KPY6; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IBA:GO_Central.
DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IBA:GO_Central.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046084; P:adenine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR CDD; cd02196; PurM; 1.
DR Gene3D; 3.30.1330.10; -; 1.
DR Gene3D; 3.90.650.10; -; 1.
DR HAMAP; MF_00741; AIRS; 1.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR016188; PurM-like_N.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR004733; PurM_cligase.
DR PANTHER; PTHR10520; PTHR10520; 1.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR SUPFAM; SSF55326; SSF55326; 1.
DR SUPFAM; SSF56042; SSF56042; 1.
DR TIGRFAMs; TIGR00878; purM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW Purine biosynthesis; Reference proteome.
FT CHAIN 1..346
FT /note="Phosphoribosylformylglycinamidine cyclo-ligase"
FT /id="PRO_0000148270"
FT HELIX 19..33
FT /evidence="ECO:0007829|PDB:3P4E"
FT STRAND 57..66
FT /evidence="ECO:0007829|PDB:3P4E"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:3P4E"
FT HELIX 84..97
FT /evidence="ECO:0007829|PDB:3P4E"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:3P4E"
FT STRAND 102..114
FT /evidence="ECO:0007829|PDB:3P4E"
FT HELIX 117..134
FT /evidence="ECO:0007829|PDB:3P4E"
FT STRAND 137..145
FT /evidence="ECO:0007829|PDB:3P4E"
FT STRAND 155..166
FT /evidence="ECO:0007829|PDB:3P4E"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:3P4E"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:3P4E"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:3P4E"
FT HELIX 195..205
FT /evidence="ECO:0007829|PDB:3P4E"
FT HELIX 218..223
FT /evidence="ECO:0007829|PDB:3P4E"
FT HELIX 230..239
FT /evidence="ECO:0007829|PDB:3P4E"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:3P4E"
FT HELIX 252..256
FT /evidence="ECO:0007829|PDB:3P4E"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:3P4E"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:3P4E"
FT HELIX 278..287
FT /evidence="ECO:0007829|PDB:3P4E"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:3P4E"
FT STRAND 302..308
FT /evidence="ECO:0007829|PDB:3P4E"
FT HELIX 310..322
FT /evidence="ECO:0007829|PDB:3P4E"
FT STRAND 327..335
FT /evidence="ECO:0007829|PDB:3P4E"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:3P4E"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:3P4E"
SQ SEQUENCE 346 AA; 36773 MW; D440BA2570E5DC0D CRC64;
MSGNNPSLSY KDAGVDIDAG NALVERIKGA VKRTRRPEVM GGLGGFGALC ELPTKYKHPV
LVSGTDGVGT KLRLALDMKK HDTIGIDLVA MCVNDLIVQG AEPLFFLDYY ATGKLDVDTA
AEVISGIADG CLQAGCALIG GETAEMPGMY EGEDYDVAGF CVGVVEKEEI IDGSKVQVGD
ALIAVGSSGP HSNGYSLVRK ILEVSKADKN ERLAGKTIGE HLLAPTKIYI KSGLKLIAEH
DIHAISHITG GGFWENIPRV LPEGTKAVID GKSWEWPVIF QWLQEKGNVT THEMYRTFNC
GVGLIIALPK DQANAAVALL QAEGETAWVI GEIAAANSNE AQVEIN
