PUR7_MYCA9
ID PUR7_MYCA9 Reviewed; 297 AA.
AC B1MHW4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase {ECO:0000255|HAMAP-Rule:MF_00137};
DE EC=6.3.2.6 {ECO:0000255|HAMAP-Rule:MF_00137};
DE AltName: Full=SAICAR synthetase {ECO:0000255|HAMAP-Rule:MF_00137};
GN Name=purC {ECO:0000255|HAMAP-Rule:MF_00137}; OrderedLocusNames=MAB_0689;
OS Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM
OS 13569 / NCTC 13031 / TMC 1543) (Mycobacterium abscessus).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacteroides; Mycobacteroides abscessus.
OX NCBI_TaxID=561007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC
RC 1543;
RX PubMed=19543527; DOI=10.1371/journal.pone.0005660;
RA Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M.,
RA Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L.,
RA Gaillard J.L.;
RT "Non mycobacterial virulence genes in the genome of the emerging pathogen
RT Mycobacterium abscessus.";
RL PLoS ONE 4:E5660-E5660(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP +
CC L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-
CC 4-carboxamido]succinate + ADP + 2 H(+) + phosphate;
CC Xref=Rhea:RHEA:22628, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58443,
CC ChEBI:CHEBI:77657, ChEBI:CHEBI:456216; EC=6.3.2.6;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00137};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
CC {ECO:0000255|HAMAP-Rule:MF_00137}.
CC -!- SIMILARITY: Belongs to the SAICAR synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00137}.
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DR EMBL; CU458896; CAM60786.1; -; Genomic_DNA.
DR RefSeq; WP_005085602.1; NZ_MLCG01000008.1.
DR PDB; 3R9R; X-ray; 1.85 A; A=1-297.
DR PDBsum; 3R9R; -.
DR AlphaFoldDB; B1MHW4; -.
DR SMR; B1MHW4; -.
DR PRIDE; B1MHW4; -.
DR EnsemblBacteria; CAM60786; CAM60786; MAB_0689.
DR GeneID; 66971075; -.
DR KEGG; mab:MAB_0689; -.
DR OMA; TKFEFGF; -.
DR UniPathway; UPA00074; UER00131.
DR Proteomes; UP000007137; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00137; SAICAR_synth; 1.
DR InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR InterPro; IPR001636; SAICAR_synth.
DR InterPro; IPR018236; SAICAR_synthetase_CS.
DR Pfam; PF01259; SAICAR_synt; 1.
DR TIGRFAMs; TIGR00081; purC; 1.
DR PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1.
DR PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis.
FT CHAIN 1..297
FT /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT synthase"
FT /id="PRO_1000095995"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:3R9R"
FT STRAND 8..13
FT /evidence="ECO:0007829|PDB:3R9R"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:3R9R"
FT STRAND 23..31
FT /evidence="ECO:0007829|PDB:3R9R"
FT HELIX 49..63
FT /evidence="ECO:0007829|PDB:3R9R"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3R9R"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:3R9R"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:3R9R"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:3R9R"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:3R9R"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:3R9R"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:3R9R"
FT HELIX 157..164
FT /evidence="ECO:0007829|PDB:3R9R"
FT HELIX 166..189
FT /evidence="ECO:0007829|PDB:3R9R"
FT STRAND 192..199
FT /evidence="ECO:0007829|PDB:3R9R"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:3R9R"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:3R9R"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:3R9R"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:3R9R"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:3R9R"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:3R9R"
FT HELIX 241..247
FT /evidence="ECO:0007829|PDB:3R9R"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:3R9R"
FT HELIX 267..285
FT /evidence="ECO:0007829|PDB:3R9R"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:3R9R"
SQ SEQUENCE 297 AA; 32730 MW; 19FA3755DD47AA6A CRC64;
MRPSLSDYQH VASGKVRELY RVDDEHLLFV ATDRISAFDF VLDTPIPDKG RILTAMSVFF
FGLLTVPNHL AGPPDDPRIP EEVLGRALLV RRLDMLPVEC VARGYLTGSG LLDYQRTGAV
CGHVLPQGLG EASRLDPPLF TPATKADIGE HDMNVDFAAV VGLVGAVRAN QLRDETIKIY
TRAAAHALHK GIILADTKFE FGVDIEGNLV LADEVFTPDS SRYWDAAHYQ PGVVQDSFDK
QFVRNWLTGP ESGWDRASDT PPPPLPDEVA VATRERYIEA YERISGLSFS DWIGPSA
