ID PUA1_MOUSE STANDARD; PRT; 452 AA. AC P28650; DT 01-DEC-1992 (REL. 24, CREATED) DT 01-DEC-1992 (REL. 24, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE ADENYLOSUCCINATE SYNTHETASE, MUSCLE ISOZYME (EC 6.3.4.4) (IMP-- DE ASPARTATE LIGASE). OS MUS MUSCULUS (MOUSE). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; RODENTIA. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=MUSCLE; RX MEDLINE; 92042206. RA GUICHERIT O.M., RUDOLPH F.B., KELLEMS R.E., COOPER B.F.; RL J. BIOL. CHEM. 266:22582-22587(1991). CC -!- PATHWAY: FIRST COMMITTED STEP IN AMP BIOSYNTHESIS. CC -!- CATALYTIC ACTIVITY: GTP + IMP + L-ASPARTATE = GDP + CC ORTHOPHOSPHATE + ADENYLOSUCCINATE. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC, AND PARTIALLY ASSOCIATED WITH CC PARTICULATE FRACTIONS. CC -!- TISSUE SPECIFICITY: HIGH LEVEL IN MUSCLE. CC -!- SIMILARITY: WITH OTHER ADENYLOSUCCINATE SYNTHETASES. 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; M74495; M74495. DR PIR; A39317; AJMSDS. DR PROSITE; PS00513; ADENYLOSUCCINATE_SYN. KW PURINE BIOSYNTHESIS; LIGASE; GTP-BINDING; MULTIGENE FAMILY. FT NP_BIND 42 48 GTP (POTENTIAL). FT ACT_SITE 174 174 BY SIMILARITY. SQ SEQUENCE 452 AA; 49472 MW; 1058833 CN; MSGTRASNDR PPGTGGVKRG RLQQEAAATG SRVTVVLGAQ WGDEGKGKVV DLLATDADIV SRCQGGNNAG HTVVVDGKEY DFHLLPSGII NTKAVSFIGN GVVIHLPGLF EEAEKNEKKG LKDWEKRLII SDRAHLVFDF HQAVDGLQEV QRQAQEGKNI GTTKKGIGPT YSSKAARTGL RICDLLSDFD EFSARFKNLA HQHQSMFPTL EIDVEGQLKR LKGFAERIRP MVRDGVYFMY EALHGPPKKV LVEGANAALL DIDFGTYPFV TSSNCTVGGV CTGLGIPPQN IGDVYGVVKA YTTRVGIGAF PTEQINEIGD LLQNRGHEWG VTTGRKRRCG WLDLMILRYA HMVNGFTALA LTKLDILDVL SEIKVGISYK LNGKRIPYFP ANQEILQKVE VEYETLPGWK ADTTGARKWE DLPPRPKATC ASWRITWVLQ SNGSALGSPE SP //