Pam

Peptidyl-glycine alpha-amidating monooxygenase

979 amino acids

Bifunctional enzyme that catalyzes the post-translational modification of inactive peptidylglycine precursors to the corresponding bioactive alpha-amidated peptides, a terminal modification in biosynthesis of many neural and endocrine peptides (By similarity). Alpha-amidation involves two sequential reactions, both of which are catalyzed by separate catalytic domains of the enzyme. The first step, catalyzed by peptidyl alpha-hydroxylating monoxygenase (PHM) domain, is the copper-, ascorbate-, and O2- dependent stereospecific hydroxylation (with S stereochemistry) at the alpha-carbon (C-alpha) of the C-terminal glycine of the peptidylglycine substrate (By similarity). The second step, catalyzed by the peptidylglycine amidoglycolate lyase (PAL) domain, is the zinc-dependent cleavage of the N-C-alpha bond, producing the alpha-amidated peptide and glyoxylate (By similarity). Similarly, catalyzes the two-step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate (Probable).

In the N-terminal section; belongs to the copper type II ascorbate-dependent monooxygenase family.

108.963 kDa

MAGRARSRLLLLLGLLALQSSCLAFRSPLSVFKRFKETTRSFSNECLGTTRPITPIDSSDFTLDIRMPGVTPKESDTYFCMSMRLPVDEEAFVIDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSLHLTRVPQPLIAGMYLMMSVNTVIPPGEKVVNSDISCHYKMYPMHVFAYRVHTHHLGKVVSGYRVRNGQWTLIGRQSPQLPQAFYPVEHPVDVAFGDILAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYMEAKHAVSFMTCTQNVAPDMFRTIPEEANIPIPVKSDMVMIHGHHKETENKEKSALIQQPKQGEEEAFEQGDFYSLLSKLLGEREDVVHVHKYNPTEKTESGSDLVAEIANVVQKKDLGRSDAREGAEHEEGGNAILVRDRIHKFHRLESTLRPAESRALSFQQPGEGPWEPELAGDFHVEEALEWPGVYLLPGQVSGVALDSKNNLVIFHRGDHVWDGNSFDSKFVYQQRGLGPIEEDTILVIDPNKAEILQSSGKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLEPRSKEGPLLVLGRSMQPGSDQNHFCQPTDVAVEPSTGAVFVSDGYCNSRIVQFSPSGKFITQWGEESSGSSPKPGQFSVPHSLALVPHLNQLCVADRENGRIQCFKTDTKEFVREIKHASFGRNVFAISYIPGFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVRKHFDMPHDIVASEDGTVYIGDAHTNTVWKFTLTESRLEVEHRSVKKAGIEVPEIKEAEAVVEPKVKNKPTSSELQKMQEKKKLIKDPGSGVPVVLITTLLVIPVVVLLAIAMFIRWKKSRAFGDHDRKLESSSGRVLGRLRGKGSSGLNLGNFFASRKGYSRKGFDRVSTEGSDQEKDEDDGSESEEEYSAPLPTPAPSS

Pam

Peptidylglycine alpha-amidating monooxygenase

976 amino acids

Bifunctional enzyme that catalyzes the post-translational modification of inactive peptidylglycine precursors to the corresponding bioactive alpha-amidated peptides, a terminal modification in biosynthesis of many neural and endocrine peptides (By similarity). Alpha-amidation involves two sequential reactions, both of which are catalyzed by separate catalytic domains of the enzyme. The first step, catalyzed by peptidyl alpha-hydroxylating monoxygenase (PHM) domain, is the copper-, ascorbate-, and O2- dependent stereospecific hydroxylation (with S stereochemistry) at the alpha-carbon (C-alpha) of the C-terminal glycine of the peptidylglycine substrate (PubMed:10079066). The second step, catalyzed by the peptidylglycine amidoglycolate lyase (PAL) domain, is the zinc-dependent cleavage of the N-C-alpha bond, producing the alpha-amidated peptide and glyoxylate (PubMed:10079066). Similarly, catalyzes the two-step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate (PubMed:10079066).

In the N-terminal section; belongs to the copper type II ascorbate-dependent monooxygenase family.

108.675 kDa

MAGRARSGLLLLLLGLLALQSSCLAFRSPLSVFKRFKETTRSFSNECLGTIGPVTPLDASDFALDIRMPGVTPKESDTYFCMSMRLPVDEEAFVIDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSVHLTRVPQPLIAGMYLMMSVDTVIPPGEKVVNADISCQYKMYPMHVFAYRVHTHHLGKVVSGYRVRNGQWTLIGRQNPQLPQAFYPVEHPVDVTFGDILAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYMEAKYALSFMTCTKNVAPDMFRTIPAEANIPIPVKPDMVMMHGHHKEAENKEKSALMQQPKQGEEEVLEQGDFYSLLSKLLGEREDVHVHKYNPTEKTESGSDLVAEIANVVQKKDLGRSDAREGAEHEEWGNAILVRDRIHRFHQLESTLRPAESRAFSFQQPGEGPWEPEPSGDFHVEEELDWPGVYLLPGQVSGVALDSKNNLVIFHRGDHVWDGNSFDSKFVYQQRGLGPIEEDTILVIDPNNAEILQSSGKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLDPHSKEGPLLILGRSMQPGSDQNHFCQPTDVAVEPSTGAVFVSDGYCNSRIVQFSPSGKFVTQWGEESSGSSPRPGQFSVPHSLALVPHLDQLCVADRENGRIQCFKTDTKEFVREIKHASFGRNVFAISYIPGFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVRKHFDMPHDIVASEDGTVYIGDAHTNTVWKFTLTEKMEHRSVKKAGIEVQEIKEAEAVVEPKVENKPTSSELQKMQEKQKLSTEPGSGVSVVLITTLLVIPVLVLLAIVMFIRWKKSRAFGDHDRKLESSSGRVLGRFRGKGSGGLNLGNFFASRKGYSRKGFDRVSTEGSDQEKDEDDGTESEEEYSAPLPKPAPSS

PAM

Peptidyl-glycine alpha-amidating monooxygenase

973 amino acids

Bifunctional enzyme that catalyzes the post-translational modification of inactive peptidylglycine precursors to the corresponding bioactive alpha-amidated peptides, a terminal modification in biosynthesis of many neural and endocrine peptides (PubMed:12699694). Alpha-amidation involves two sequential reactions, both of which are catalyzed by separate catalytic domains of the enzyme. The first step, catalyzed by peptidyl alpha-hydroxylating monoxygenase (PHM) domain, is the copper-, ascorbate-, and O2- dependent stereospecific hydroxylation (with S stereochemistry) at the alpha-carbon (C-alpha) of the C-terminal glycine of the peptidylglycine substrate (PubMed:12699694). The second step, catalyzed by the peptidylglycine amidoglycolate lyase (PAL) domain, is the zinc-dependent cleavage of the N-C-alpha bond, producing the alpha-amidated peptide and glyoxylate (PubMed:12699694). Similarly, catalyzes the two-step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate (By similarity).

In the N-terminal section; belongs to the copper type II ascorbate-dependent monooxygenase family.

108.332 kDa

MAGRVPSLLVLLVFPSSCLAFRSPLSVFKRFKETTRPFSNECLGTTRPVVPIDSSDFALDIRMPGVTPKQSDTYFCMSMRIPVDEEAFVIDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNNKDCSGVSLHLTRLPQPLIAGMYLMMSVDTVIPAGEKVVNSDISCHYKNYPMHVFAYRVHTHHLGKVVSGYRVRNGQWTLIGRQSPQLPQAFYPVGHPVDVSFGDLLAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYMEAKHAVSFMTCTQNVAPDMFRTIPPEANIPIPVKSDMVMMHEHHKETEYKDKIPLLQQPKREEEEVLDQGDFYSLLSKLLGEREDVVHVHKYNPTEKAESESDLVAEIANVVQKKDLGRSDAREGAEHERGNAILVRDRIHKFHRLVSTLRPPESRVFSLQQPPPGEGTWEPEHTGDFHMEEALDWPGVYLLPGQVSGVALDPKNNLVIFHRGDHVWDGNSFDSKFVYQQIGLGPIEEDTILVIDPNNAAVLQSSGKNLFYLPHGLSIDKDGNYWVTDVALHQVFKLDPNNKEGPVLILGRSMQPGSDQNHFCQPTDVAVDPGTGAIYVSDGYCNSRIVQFSPSGKFITQWGEESSGSSPLPGQFTVPHSLALVPLLGQLCVADRENGRIQCFKTDTKEFVREIKHSSFGRNVFAISYIPGLLFAVNGKPHFGDQEPVQGFVMNFSNGEIIDIFKPVRKHFDMPHDIVASEDGTVYIGDAHTNTVWKFTLTEKLEHRSVKKAGIEVQEIKEAEAVVETKMENKPTSSELQKMQEKQKLIKEPGSGVPVVLITTLLVIPVVVLLAIAIFIRWKKSRAFGDSEHKLETSSGRVLGRFRGKGSGGLNLGNFFASRKGYSRKGFDRLSTEGSDQEKEDDGSESEEEYSAPLPALAPSSS

PAM

Peptidyl-glycine alpha-amidating monooxygenase

972 amino acids

Bifunctional enzyme that catalyzes the post-translational modification of inactive peptidylglycine precursors to the corresponding bioactive alpha-amidated peptides, a terminal modification in biosynthesis of many neural and endocrine peptides (PubMed:2059626). Alpha-amidation involves two sequential reactions, both of which are catalyzed by separate catalytic domains of the enzyme. The first step, catalyzed by peptidyl alpha-hydroxylating monoxygenase (PHM) domain, is the copper-, ascorbate-, and O2- dependent stereospecific hydroxylation (with S stereochemistry) at the alpha-carbon (C-alpha) of the C-terminal glycine of the peptidylglycine substrate (PubMed:2059626). The second step, catalyzed by the peptidylglycine amidoglycolate lyase (PAL) domain, is the zinc-dependent cleavage of the N-C-alpha bond, producing the alpha-amidated peptide and glyoxylate (PubMed:2059626). Similarly, catalyzes the two-step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate (By similarity).

In the N-terminal section; belongs to the copper type II ascorbate-dependent monooxygenase family.

108.177 kDa

MAGFRSLLVLLLVFPSGCVGFRSPLSVFKRFKETTRSFSNECLGTTRPVIPIDSSDFALDIRMPGVTPKQSDTYFCMSVRLPMDEEAFVIDFKPRASMDTVHHMLLFGCNMPASTGNYWFCDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSLHLTRLPQPLIAGMYLMMSVDTVIPPGGKVVNSDISCHYKKYPMHVFAYRVHTHHLGKVVSGYRVRNGQWTLIGRQSPQLPQAFYPVEHPVDVSFGDILAARCVFTGEGRTEVTHIGGTSSDEMCNLYIMYYMEAKHAVSFMTCTQNVAPDIFRTIPPEANIPIPVKSDMVMMHGHHKETENKDKTSLLQQPKREEEGVLEQGDFYSLLSKLLGEREDVVHVHKYNPTEKAESESDLVAEIANVVQKKDLGRSDTRESAEQERGNAILVRDRIHKFHRLVSTLRPAESRVLSLQQPLPGEGTWEPEHTGDFHVEEALDWPGVYLLPGQVSGVALDPQNNLVIFHRGDHVWDGNSFDSKFVYQQRGLGPIEEDTILVIDPNNAAVLQSSGKNLFYLPHGLSIDKDGNYWVTDVALHQVFKLDPKSKEGPLLTLGRSMQPGSDQNHFCQPTDVAVDPDTGTIYVSDGYCNSRLVQFSPSGKFITQWGEASLESSPKPGQFRVPHSLALVPPLGQLCVADRENGRIQCFKTDTKEFVREIKHPSFGRNVFAISYIPGLLFAVNGKPYFEDQEPVQGFVMNFSSGEIIDVFKPVRKHFDMPHDIAASEDGTVYVGDAHTNTVWKFTSTEKMEHRSVKKAGIEVQEIKESEAVVETKMENKPASSELQKIQEKQKLVKEPGSGVPAVLITTLLVIPVVVLLAIALFIRWKKSRAFGDSERKLEASSGRVLGRLRGKGGGGLNLGNFFASRKGYSRKGFDRLSTEGSDQEKDEDASESEEEYSAPPPAPAPSS

pam

Phenylalanine aminomutase (L-beta-phenylalanine forming)

698 amino acids

Phenylalanine aminomutase that catalyzes the rearrangement of L-phenylalanine to R-beta-phenylalanine. Catalyzes the first committed step in the biosynthesis of the side chain of the alkaloid taxol (paclitaxel), a widely-used compound with antitumor activity. Also has low phenylalanine ammonia-lyase activity.

Belongs to the PAL/histidase family.

76.532 kDa

MGFAVESRSHVKDILGLINTFNEVKKITVDGTTPITVAHVAALARRHDVKVALEAEQCRARVETCSSWVQRKAEDGADIYGVTTGFGACSSRRTNQLSELQESLIRCLLAGVFTKGCASSVDELPATATRSAMLLRLNSFTYGCSGIRWEVMEALEKLLNSNVSPKVPLRGSVSASGDLIPLAYIAGLLIGKPSVVARIGDDVEVPAPEALSRVGLRPFKLQAKEGLALVNGTSFATALASTVMYDANVLLLLVETLCGMFCEVIFGREEFAHPLIHKVKPHPGQIESAELLEWLLRSSPFQDLSREYYSIDKLKKPKQDRYALRSSPQWLAPLVQTIRDATTTVETEVNSANDNPIIDHANDRALHGANFQGSAVGFYMDYVRIAVAGLGKLLFAQFTELMIEYYSNGLPGNLSLGPDLSVDYGLKGLDIAMAAYSSELQYLANPVTTHVHSAEQHNQDINSLALISARKTEEALDILKLMIASHLTAMCQAVDLRQLEEALVKVVENVVSTLADECGLPNDTKARLLYVAKAVPVYTYLESPCDPTLPLLLGLEQSCFGSILALHKKDGIETDTLVDRLAEFEKRLSDRLENEMTAVRVLYEKKGHKTADNNDALVRIQGSRFLPFYRFVREELDTGVMSARREQTPQEDVQKVFDAIADGRITVPLLHCLQGFLGQPNGCANGVESFQSVWNKSA

pam

Phenylalanine aminomutase (L-beta-phenylalanine forming)

687 amino acids

Phenylalanine aminomutase that catalyzes the rearrangement of L-phenylalanine to R-beta-phenylalanine. Catalyzes the first committed step in the biosynthesis of the side chain of the alkaloid taxol (paclitaxel), a widely-used compound with antitumor activity. Has also low phenylalanine ammonia-lyase activity and can catalyze the amination of trans-cinnamate.

Belongs to the PAL/histidase family.

75.332 kDa

MGFAVESRSHVKDILGLINAFNEVKKITVDGTTPITVAHVAALARRHDVKVALEAEQCRARVETCSSWVQRKAEDGADIYGVTTGFGACSSRRTNRLSELQESLIRCLLAGVFTKGCAPSVDELPATATRSAMLLRLNSFTYGCSGIRWEVMEALEKLLNSNVSPKVPLRGSVSASGDLIPLAYIAGLLIGKPSVIARIGDDVEVPAPEALSRVGLRPFKLQAKEGLALVNGTSFATAVASTVMYDANVLLLLVETLCGMFCEVIFGREEFAHPLIHKVKPHPGQIESAELLEWLLRSSPFQELSREYYSIDKLKKPKQDRYALRSSPQWLAPLVQTIRDATTTVETEVNSANDNPIIDHANDRALHGANFQGSAVGFYMDYVRIAVAGLGKLLFAQFTELMIEYYSNGLPGNLSLGPDLSVDYGLKGLDIAMAAYSSELQYLANPVTTHVHSAEQHNQDINSLALISARKTEEALDILKLMIASHLTAMCQAVDLRQLEEALVKVVENVVSTLADECGLPNDTKARLLYVAKAVPVYTYLESPCDPTLPLLLGLKQSCFDTILALHKKDGIETDTLVDRLAEFEKRLSDRLENEMTAVRVLYEKKGHKTADNNDALVRIQGSKFLPFYRFVREELDTGVMSARREQTPQEDVQKVFDAIADGRITVPLLHCLQGFLGQPNGCANGV

pam

Plasminogen-binding group A streptococcal M-like protein PAM

388 amino acids

Binds to human plasminogen (and plasmin) via its kringle repeats. Also binds to albumin, immunoglobulin G and fibrinogen. Could provide the bacteria with a mechanism for invasion, as streptococcal-bound plasmin could permit tissue penetration.

Belongs to the M protein family.

43.629 kDa

single

RKLKTGTASVAVALTVVGAGLASQTEVKANRADDARNEVLRGNLVRAELWYRQIQENDQLKLENKGLKTDLREKEEELQGLKDDVEKLTADAELQRLKNERHEEAELERLKSERHDHDKKEAERKALEDKLADKQEHLNGALRYINEKEAEAKEKEAEQKKLKEEKQISDASRQGLRRDLDASREAKKQVEKDLANLTAELDKVKEEKQISDASRQGLRRDLDASREAKKQVEKGLANLTAELDKVKEEKQISDASRQGLRRDLDASREAKKQVEKALEEANSKLAALEKLNKELEESKKLTEKEKAELQAKLEAEAKALKEQLAKQAEELAKLRAEKASDSQTPDAKPGNKAVPGKGQAPQAGTKPNQNKAPMKETKRQLPSTGETT