PUR7_EHRCR
ID PUR7_EHRCR Reviewed; 242 AA.
AC Q2GHH2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=ECH_0290;
OS Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=205920;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC CRL-10679 / Arkansas;
RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C.,
RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C.,
RA Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D.,
RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT "Comparative genomics of emerging human ehrlichiosis agents.";
RL PLoS Genet. 2:208-222(2006).
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; CP000236; ABD45002.1; -; Genomic_DNA.
DR RefSeq; WP_006011312.1; NC_007799.1.
DR PDB; 3KRE; X-ray; 1.80 A; A=1-242.
DR PDBsum; 3KRE; -.
DR AlphaFoldDB; Q2GHH2; -.
DR SMR; Q2GHH2; -.
DR STRING; 205920.ECH_0290; -.
DR EnsemblBacteria; ABD45002; ABD45002; ECH_0290.
DR KEGG; ech:ECH_0290; -.
DR eggNOG; COG0152; Bacteria.
DR HOGENOM; CLU_061495_2_0_5; -.
DR OMA; EFCYKND; -.
DR OrthoDB; 1345271at2; -.
DR UniPathway; UPA00074; UER00131.
DR EvolutionaryTrace; Q2GHH2; -.
DR Proteomes; UP000008320; 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 GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
DR CDD; cd01415; SAICAR_synt_PurC; 1.
DR HAMAP; MF_00137; SAICAR_synth; 1.
DR InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR InterPro; IPR033934; SAICAR_synt_PurC.
DR InterPro; IPR001636; SAICAR_synth.
DR InterPro; IPR018236; SAICAR_synthetase_CS.
DR Pfam; PF01259; SAICAR_synt; 1.
DR TIGRFAMs; TIGR00081; purC; 1.
DR PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..242
FT /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT synthase"
FT /id="PRO_1000018702"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:3KRE"
FT STRAND 11..17
FT /evidence="ECO:0007829|PDB:3KRE"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:3KRE"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:3KRE"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:3KRE"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:3KRE"
FT HELIX 46..63
FT /evidence="ECO:0007829|PDB:3KRE"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:3KRE"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:3KRE"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:3KRE"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:3KRE"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:3KRE"
FT STRAND 112..122
FT /evidence="ECO:0007829|PDB:3KRE"
FT TURN 125..128
FT /evidence="ECO:0007829|PDB:3KRE"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:3KRE"
FT HELIX 145..168
FT /evidence="ECO:0007829|PDB:3KRE"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:3KRE"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:3KRE"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:3KRE"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:3KRE"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:3KRE"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:3KRE"
FT HELIX 225..236
FT /evidence="ECO:0007829|PDB:3KRE"
SQ SEQUENCE 242 AA; 28036 MW; 12A85540BC1587E4 CRC64;
MENKEKIYEG KAKIIFATLN PLEVIQHFKD EITAFNNKKA AIIHEKGILN NYISSFLMKK
LIDKGIKTHF ISLLNQREQL VKKITIIPIE VVIRNLAAGN FSKRFQIADG TPFKSPIIEF
YYKNDELSDP MVSEGHILSF QWLTNQELEK IKILSLKINN ILSELFFNVG IKLVDFKLEF
GKLHNDEQSD LFLADEISPD TCRLWDISTN KRLDKDRYRL NLGNVIEGYR EVAHKLNAIP
NL
