ID PURK_MYCLE STANDARD; PRT; 439 AA. AC P46701; DT 01-NOV-1995 (REL. 32, CREATED) DT 01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE ATPASE SUBUNIT (EC 4.1.1.21) DE (AIR CARBOXYLASE) (AIRC). GN PURK OR B1308_F1_32. OS MYCOBACTERIUM LEPRAE. OC PROKARYOTA; FIRMICUTES; ACTINOMYCETALES; MYCOBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RA SMITH D.R., ROBISON K.; RL SUBMITTED (MAR-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: POSSESSES AN ATPASE ACTIVITY THAT IS DEPENDENT ON THE CC PRESENCE OF AIR (AMINOIMIDAZOLE RIBONUCLEOTIDE). THE ASSOCIATION CC OF PURK AND PURE PRODUCE AN ENZYME COMPLEX CAPABLE OF CONVERTING CC AIR TO CAIR EFFICIENTLY UNDER PHYSIOLOGICAL CONDITION CC (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: 1-(5-PHOSPHORIBOSYL)-5-AMINO-4-IMIDAZOLE- CC CARBOXYLATE = 1-(5-PHOSPHORIBOSYL)-5-AMINOIMIDAZOLE + CO(2). CC -!- PATHWAY: SIXTH STEP IN DE NOVO PURINE BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SIMILARITY: TO OTHER BACTERIAL PURK, ALSO TO AIR CARBOXYLASE FROM CC FUNGI. 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; U00012; G466859; -. KW PURINE BIOSYNTHESIS; LYASE; DECARBOXYLASE. SQ SEQUENCE 439 AA; 47306 MW; 5539C957 CRC32; MMAVPSRCSL GVAPLVAMVG GGQLARMTHQ AAIALGQTLR VLATAADEPA AQVTPDVVIG SHTDLEDLRR VALGADALTF DHEHVPTELL DKLVAEGINV APSPQALVHA QDKLVMRRRL AALGAAMPRF MALDSVDDLA EIDAFAQRLT GSKDAPMVVK AVRGGYDGRG VQMVRDSAHA REVASGYLVD GMPVLVEERV ELRRELSALV ARSPFGQGAA WPVVETVQRD GICVLVVAPA LALADDLASA AQQLALRLAA ELGVVGVFAV ELFETADGAL LVNELAMRPH NSGHWTMDGA RTSQFEQHLR AVLDYPLGET DAVAPVTVMV NVLGAPQPPT LSVVTMDERL HHLFARMPDA RVHLYDKVER PGRKVGHINF RGTDKDRKNP TKLRERAELA AHWLSHGQWT DGWDPHRAGD DVVEISLACG GRNDAQRQR //