eF-site ID 3umm-A PDB Code 3umm Chain A click to enlarge Title Formylglycinamide ribonucleotide amidotransferase from Salmonella typhimurium: Role of the ATP complexation and glutaminase domain in catalytic coupling Classification LIGASE Compound Phosphoribosylformylglycinamidine synthase Source ORGANISM_SCIENTIFIC: Salmonella enterica subsp. enterica serovar Typhimurium; Sequence A:  GLVPRGSHMMEILRGSPALSAFRINKLLARFQAANLQVHN IYAEYVHFADLNAPLNDSEQAQLTRLLQYGPALSSHTPAG KLLLVTPRPGTISPWSSKATDIAHNCGLQQVDRLERGVAY YIEASTLTAEQWRQVAAELHDRMMETVFSSLTDAEKLFIH HQPAPVSSVDLLGEGRQALIDANLRLGLALAEDEIDYLQE AFTKLGRNPNDIELYMFAQANSEHCRHKIFNADWIIDGKP QPKSLFKMIKNTFETTPDYVLSAYKDNAAVMEGSAVGRYF ADHNTGRYDFHQEPAHILMKVETHNHPTAISPWPGAATGS GGEIRDEGATGRGAKPKAGLVGFSVSNLRIPGFEQPWEED FGKPERIVTALDIMTEGPLGGAAFNNEFGRPALTGYFRTY EEKVNSHNGEELRGYHKPIMLAGGIGNIRADHVQKGEIVV GAKLIVLGGPAMNIGDFASVQRDNPEMERRCQEVIDRCWQ LGDANPILFIHDVGAGGLSNAMPELVSDGGRGGKFELRDI LSDEPGMSPLEIWCNESQERYVLAVAADQLPLFDELCKRE RAPYAVIGDATEEQHLSLHDNHFDNQPIDLPLDVLLGKTP KMTRDVQTLKAKGDALNRADITIADAVKRVLHLPTVAEKT FLVTIGDRTVTGMVARDQMVGPWQVPVADCAVTTASLDSY YGEAMSIGERAPVALLDFAASARLAVGEALTNIAATQIGD IKRIKLSANWMAAAGHPGEDAGLYDAVKAVGEELCPQLGL TIPVGKDSMSMKTRWQEGNEQREMTSPLSLVISAFARVED VRHTLTPQLSTEDNALLLIDLGKGHNALGATALAQVYRQL GDKPADVRDVAQLKGFYDAMQALVAARKLLAWHDRSDGGL LVTLAEMAFAGHCGVQVDIAALGDDHLAALFNEELGGVIQ VRAEDRDAVEALLAQYGLADCVHYLGQALAGDRFVITAND QTVFSESRTTLRVWWAETTWQMQRLRDNPQCADQEHEAKA NDTDPGLNVKLSFDINEDIAAPYIATGARPKVAVLREQGV NSHVEMAAAFHRAGFDAIDVHMSDLLGGRIGLGNFHALVA CGGFSYGDVLGAGEGWAKSILFNHRVRDEFETFFHRPQTL ALGVXNGCQMMSNLRELIPGSELWPRFVRNHSDRFEARFS LVEVTQSPSLLLQGMVGSQMPIAVSHGEGRVEVRDDAHLA ALESKGLVALRYVDNFGKVTETYPANPNGSPNGITAVTTE NGRVTIMMPHPERVFRTVANSWHPENWGEDSPWMRIFRNA RKQLG Description (1)  Phosphoribosylformylglycinamidine synthase (E.C.6.3.5.3) Functional site 1) chain A residue 219 type sequence H description BINDING SITE FOR RESIDUE ANP A 2001 source : AC1 2) chain A residue 222 type sequence F description BINDING SITE FOR RESIDUE ANP A 2001 source : AC1 3) chain A residue 258 type sequence D description BINDING SITE FOR RESIDUE ANP A 2001 source : AC1 4) chain A residue 259 type sequence N description BINDING SITE FOR RESIDUE ANP A 2001 source : AC1 5) chain A residue 292 type sequence K description BINDING SITE FOR RESIDUE ANP A 2001 source : AC1 6) chain A residue 294 type sequence E description BINDING SITE FOR RESIDUE ANP A 2001 source : AC1 7) chain A residue 318 type sequence D description BINDING SITE FOR RESIDUE ANP A 2001 source : AC1 8) chain A residue 502 type sequence D description BINDING SITE FOR RESIDUE ANP A 2001 source : AC1 9) chain A residue 774 type sequence V description BINDING SITE FOR RESIDUE ANP A 2001 source : AC1 10) chain A residue 775 type sequence G description BINDING SITE FOR RESIDUE ANP A 2001 source : AC1 11) chain A residue 776 type sequence K description BINDING SITE FOR RESIDUE ANP A 2001 source : AC1 12) chain A residue 777 type sequence D description BINDING SITE FOR RESIDUE ANP A 2001 source : AC1 13) chain A residue 386 type sequence T description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 14) chain A residue 387 type sequence G description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 15) chain A residue 388 type sequence Y description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 16) chain A residue 389 type sequence F description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 17) chain A residue 649 type sequence K description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 18) chain A residue 668 type sequence Q description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 19) chain A residue 676 type sequence P description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 20) chain A residue 678 type sequence A description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 21) chain A residue 679 type sequence D description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 22) chain A residue 718 type sequence E description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 23) chain A residue 722 type sequence N description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 24) chain A residue 886 type sequence S description BINDING SITE FOR RESIDUE ADP A 2005 source : AC2 25) chain A residue 718 type sequence E description BINDING SITE FOR RESIDUE MG A 2006 source : AC3 26) chain A residue 886 type sequence S description BINDING SITE FOR RESIDUE MG A 2007 source : AC4 27) chain A residue 679 type sequence D description BINDING SITE FOR RESIDUE MG A 2008 source : AC5 28) chain A residue 722 type sequence N description BINDING SITE FOR RESIDUE MG A 2008 source : AC5 29) chain A residue 884 type sequence D description BINDING SITE FOR RESIDUE MG A 2008 source : AC5 30) chain A residue 216 type sequence H description BINDING SITE FOR RESIDUE SO4 A 2002 source : AC6 31) chain A residue 295 type sequence T description BINDING SITE FOR RESIDUE SO4 A 2002 source : AC6 32) chain A residue 297 type sequence N description BINDING SITE FOR RESIDUE SO4 A 2002 source : AC6 33) chain A residue 409 type sequence K description BINDING SITE FOR RESIDUE SO4 A 2002 source : AC6 34) chain A residue 778 type sequence S description BINDING SITE FOR RESIDUE SO4 A 2002 source : AC6 35) chain A residue 12 type sequence S description BINDING SITE FOR RESIDUE SO4 A 2009 source : AC7 36) chain A residue 13 type sequence A description BINDING SITE FOR RESIDUE SO4 A 2009 source : AC7 37) chain A residue 14 type sequence F description BINDING SITE FOR RESIDUE SO4 A 2009 source : AC7 38) chain A residue 998 type sequence N description BINDING SITE FOR RESIDUE SO4 A 2009 source : AC7 39) chain A residue 1161 type sequence H description BINDING SITE FOR RESIDUE SO4 A 2009 source : AC7 40) chain A residue 1135 type ACT_SITE sequence X description Nucleophile => ECO:0000255|HAMAP-Rule:MF_00419 source Swiss-Prot : SWS_FT_FI1 41) chain A residue 1260 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00419 source Swiss-Prot : SWS_FT_FI2 42) chain A residue 1262 type ACT_SITE sequence E description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00419 source Swiss-Prot : SWS_FT_FI2 43) chain A residue 307 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00419 source Swiss-Prot : SWS_FT_FI3 44) chain A residue 386 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI4 45) chain A residue 678 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI4 46) chain A residue 886 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI4 47) chain A residue 679 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00419, ECO:0000269|PubMed:15301531, ECO:0000269|PubMed:22683785, ECO:0000269|PubMed:24223728 source Swiss-Prot : SWS_FT_FI5 48) chain A residue 718 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00419, ECO:0000269|PubMed:15301531, ECO:0000269|PubMed:22683785, ECO:0000269|PubMed:24223728 source Swiss-Prot : SWS_FT_FI5 49) chain A residue 722 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00419, ECO:0000269|PubMed:15301531, ECO:0000269|PubMed:22683785, ECO:0000269|PubMed:24223728 source Swiss-Prot : SWS_FT_FI5 50) chain A residue 884 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00419, ECO:0000269|PubMed:15301531, ECO:0000269|PubMed:22683785, ECO:0000269|PubMed:24223728 source Swiss-Prot : SWS_FT_FI5

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