Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes; This superfamily (also known as the C-N hydrolase superfamily) contains hydrolases that break carbon-nitrogen bonds; it includes nitrilases, cyanide dihydratases, aliphatic amidases, N-terminal amidases, beta-ureidopropionases, biotinidases, pantotheinase, N-carbamyl-D-amino acid amidohydrolases, the glutaminase domain of glutamine-dependent NAD+ synthetase, apolipoprotein N-acyltransferases, and N-carbamoylputrescine amidohydrolases, among others. These enzymes depend on a Glu-Lys-Cys catalytic triad, and work through a thiol acylenzyme intermediate. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. These oligomers include dimers, tetramers, hexamers, octamers, tetradecamers, octadecamers, as well as variable length helical arrangements and homo-oligomeric spirals. These proteins have roles in vitamin and co-enzyme metabolism, in detoxifying small molecules, in the synthesis of signaling molecules, and in the post-translational modification of proteins. They are used industrially, as biocatalysts in the fine chemical and pharmaceutical industry, in cyanide remediation, and in the treatment of toxic effluent. This superfamily has been classified previously in the literature, based on global and structure-based sequence analysis, into thirteen different enzyme classes (referred to as 1-13). This hierarchy includes those thirteen classes and a few additional subfamilies. A putative distant relative, the plasmid-borne TraB family, has not been included in the hierarchy.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  26 FIAAVYEHAVILPNKTetpvsqeDALNLMNENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRETVFPYLEDIPDPQV 105
Cdd:cd07567     1 YIAAVVEHHPILSPDP-------DALQIMEKNLDIYEEIIKSAAKQGADIIVFPEDGLTGFIFTRFVIYPFLEDVPDPEV 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844083952 106 NWIPCQDPHRFGHTPVQARLSCLAKDNSIYVLANLGDKKPCNSRDSTCPPNGYFQYNTNVVYNTEGKLVARYHKV 180
Cdd:cd07567    74 NWNPCLDPDRFDYTEVLQRLSCAARENSIYVVANLGEKQPCDSSDPHCPPDGRYQYNTNVVFDRDGTLIARYRKY 148

biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin recycling. Biotinidase (EC 3.5.1.12) has both a hydrolase and a transferase activity. It hydrolyzes free biocytin or small biotinyl-peptides produced during the proteolytic degradation of biotin-dependent carboxylases, to release free biotin (vitamin H), and it can transfer biotin to acceptor molecules such as histones. Biotinidase deficiency in humans is an autosomal recessive disorder characterized by neurological and cutaneous symptoms. This subgroup includes the three human vanins, vanin1-3. Vanins are ectoenzymes, Vanin-1, and -2 are membrane associated, vanin-3 is secreted. They are pantotheinases (EC 3.5.1.92, pantetheine hydrolase), which convert pantetheine, to pantothenic acid (vitamin B5) and cysteamine (2-aminoethanethiol, a potent anti-oxidant). They are potential targets for therapeutic intervention in inflammatory disorders. Vanin-1 deficient mice lacking free cysteamine are less susceptible to intestinal inflammation, and expression of vanin-1 and -3 is induced as part of the inflammatory-regenerative differentiation program of human epidermis. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 4. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  26 FIAAVYEHAVILPNKTetpvsqeDALNLMNENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRETVFPYLEDIPDPQV 105
Cdd:cd07567     1 YIAAVVEHHPILSPDP-------DALQIMEKNLDIYEEIIKSAAKQGADIIVFPEDGLTGFIFTRFVIYPFLEDVPDPEV 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844083952 106 NWIPCQDPHRFGHTPVQARLSCLAKDNSIYVLANLGDKKPCNSRDSTCPPNGYFQYNTNVVYNTEGKLVARYHKV 180
Cdd:cd07567    74 NWNPCLDPDRFDYTEVLQRLSCAARENSIYVVANLGEKQPCDSSDPHCPPDGRYQYNTNVVFDRDGTLIARYRKY 148

Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  56 ENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRETVFPYLEDIPDPQVnwipcqdphrfghtpvqARLSCLAKDNSIY 135
Cdd:COG0388    18 ANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDGPAL-----------------AALAELARELGIA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1844083952 136 VLANLGDKkpcnsrdstCPPNGYfqYNTNVVYNTEGKLVARYHKV 180
Cdd:COG0388    81 VVVGLPER---------DEGGRL--YNTALVIDPDGEILGRYRKI 114

apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the lgt/lsp/lnt system which is found broadly in bacteria but not in archaea. This model represents one component of the "lipoprotein lgt/lsp/lnt system" genome property. [Protein fate, Protein modification and repair]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  34 AVILPNkteTPVSQEDALNLMNENIDILETAIKQAAEQgARIIVTPEdalygwkftreTVFPYLEDIPdPQVNwipcqdp 113
Cdd:TIGR00546 163 ALVQPN---IPQDLKFDSEGLEAILEILTSLTKQAVEK-PDLVVWPE-----------TAFPFDLENS-PQKL------- 219

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083952 114 hrfghtpvQARLSCLAKDNSIYVLANLgdkkpcnsrDSTCPPNGYFQYNTNVVYNTEGKLVARYHKV 180
Cdd:TIGR00546 220 --------ADRLKLLVLSKGIPILIGA---------PDAVPGGPYHYYNSAYLVDPGGEVVQRYDKV 269

biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin recycling. Biotinidase (EC 3.5.1.12) has both a hydrolase and a transferase activity. It hydrolyzes free biocytin or small biotinyl-peptides produced during the proteolytic degradation of biotin-dependent carboxylases, to release free biotin (vitamin H), and it can transfer biotin to acceptor molecules such as histones. Biotinidase deficiency in humans is an autosomal recessive disorder characterized by neurological and cutaneous symptoms. This subgroup includes the three human vanins, vanin1-3. Vanins are ectoenzymes, Vanin-1, and -2 are membrane associated, vanin-3 is secreted. They are pantotheinases (EC 3.5.1.92, pantetheine hydrolase), which convert pantetheine, to pantothenic acid (vitamin B5) and cysteamine (2-aminoethanethiol, a potent anti-oxidant). They are potential targets for therapeutic intervention in inflammatory disorders. Vanin-1 deficient mice lacking free cysteamine are less susceptible to intestinal inflammation, and expression of vanin-1 and -3 is induced as part of the inflammatory-regenerative differentiation program of human epidermis. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 4. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  26 FIAAVYEHAVILPNKTetpvsqeDALNLMNENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRETVFPYLEDIPDPQV 105
Cdd:cd07567     1 YIAAVVEHHPILSPDP-------DALQIMEKNLDIYEEIIKSAAKQGADIIVFPEDGLTGFIFTRFVIYPFLEDVPDPEV 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844083952 106 NWIPCQDPHRFGHTPVQARLSCLAKDNSIYVLANLGDKKPCNSRDSTCPPNGYFQYNTNVVYNTEGKLVARYHKV 180
Cdd:cd07567    74 NWNPCLDPDRFDYTEVLQRLSCAARENSIYVVANLGEKQPCDSSDPHCPPDGRYQYNTNVVFDRDGTLIARYRKY 148

Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes; This superfamily (also known as the C-N hydrolase superfamily) contains hydrolases that break carbon-nitrogen bonds; it includes nitrilases, cyanide dihydratases, aliphatic amidases, N-terminal amidases, beta-ureidopropionases, biotinidases, pantotheinase, N-carbamyl-D-amino acid amidohydrolases, the glutaminase domain of glutamine-dependent NAD+ synthetase, apolipoprotein N-acyltransferases, and N-carbamoylputrescine amidohydrolases, among others. These enzymes depend on a Glu-Lys-Cys catalytic triad, and work through a thiol acylenzyme intermediate. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. These oligomers include dimers, tetramers, hexamers, octamers, tetradecamers, octadecamers, as well as variable length helical arrangements and homo-oligomeric spirals. These proteins have roles in vitamin and co-enzyme metabolism, in detoxifying small molecules, in the synthesis of signaling molecules, and in the post-translational modification of proteins. They are used industrially, as biocatalysts in the fine chemical and pharmaceutical industry, in cyanide remediation, and in the treatment of toxic effluent. This superfamily has been classified previously in the literature, based on global and structure-based sequence analysis, into thirteen different enzyme classes (referred to as 1-13). This hierarchy includes those thirteen classes and a few additional subfamilies. A putative distant relative, the plasmid-borne TraB family, has not been included in the hierarchy.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  54 MNENIDILETAIKQAAEQGARIIVTPEDALYGWKF-TRETVFPYLEDIPDPQVNWipcqdphrfghtpvqarLSCLAKDN 132
Cdd:cd07197    13 VEANLAKALRLIKEAAEQGADLIVLPELFLTGYSFeSAKEDLDLAEELDGPTLEA-----------------LAELAKEL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1844083952 133 SIYVLANLGDKKPCNsrdstcppngyfQYNTNVVYNTEGKLVARYHKV 180
Cdd:cd07197    76 GIYIVAGIAEKDGDK------------LYNTAVVIDPDGEIIGKYRKI 111

Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  56 ENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRETVFPYLEDIPDPQVnwipcqdphrfghtpvqARLSCLAKDNSIY 135
Cdd:COG0388    18 ANLAKIEELIREAAAQGADLVVFPELFLTGYPPEDDDLLELAEPLDGPAL-----------------AALAELARELGIA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1844083952 136 VLANLGDKkpcnsrdstCPPNGYfqYNTNVVYNTEGKLVARYHKV 180
Cdd:COG0388    81 VVVGLPER---------DEGGRL--YNTALVIDPDGEILGRYRKI 114

N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known as N-carbamoylputrescine amidase and carbamoylputrescine hydrolase) converts N-carbamoylputrescine to putrescine, a step in polyamine biosynthesis in plants and bacteria. This subgroup includes Arabidopsis thaliana CPA, also known as nitrilase-like 1 (NLP1), and Pseudomonas aeruginosa AguB. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 11. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer; P. aeruginosa AugB is a homohexamer, Arabidopsis thaliana NLP1 is a homooctomer.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  56 ENIDILETAIKQAAEQGARIIVTPE--DALYGWKFTRETVFPYLEDIpdpqvnwipcqDPHrfghtPVQARLSCLAKDNS 133
Cdd:cd07573    16 ANLAKAEELVREAAAQGAQIVCLQElfETPYFCQEEDEDYFDLAEPP-----------IPG-----PTTARFQALAKELG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1844083952 134 IYVLANLGDKKpcnsrdstcPPNGYfqYNTNVVYNTEGKLVARYHKV 180
Cdd:cd07573    80 VVIPVSLFEKR---------GNGLY--YNSAVVIDADGSLLGVYRKM 115

Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. The family includes: Nitrilase EC:3.5.5.1, Aliphatic amidase EC:3.5.1.4, Biotidinase EC:3.5.1.12, Beta-ureidopropionase EC:3.5.1.6. Nitrilase-related proteins generally have a conserved E-K-C catalytic triad, and are multimeric alpha-beta-beta-alpha sandwich proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  56 ENIDILETAIKQAAEQGARIIVTPEDALYGWKFTREtVFPYLEDIPdpqvnwipcqdphrfghTPVQARLSCLAKDNSIY 135
Cdd:pfam00795  16 ANLQKALELIEEAARYGADLIVLPELFITGYPCWAH-FLEAAEVGD-----------------GETLAGLAALARKNGIA 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1844083952 136 VLANLGDKKPCNSRdstcppngyfQYNTNVVYNTEGKLVARYHKV 180
Cdd:pfam00795  78 IVIGLIERWLTGGR----------LYNTAVLLDPDGKLVGKYRKL 112

First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); Members of this subgroup have two nitrilase domains. This is the first of those two domains. The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  56 ENIDILETAIKQAAEQGARIIVTPEDAL--YGWkFTRETVFPYLEDIPDpqvnwipcqdphrfghtPVQARLSCLAKDNS 133
Cdd:cd07578    17 RNIERLLALCEEAARAGARLIVTPEMATtgYCW-YDRAEIAPFVEPIPG-----------------PTTARFAELAREHD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1844083952 134 IYVLANLGDKKpcnsrdstcPPNGYFqYNTNVVYNTEGkLVARYHK 179
Cdd:cd07578    79 CYIVVGLPEVD---------SRSGIY-YNSAVLIGPSG-VIGRHRK 113

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  45 VSQEDALNLMNENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRE-TVFPYL-EDIPDPQVNWipcqdphrfghtpvq 122
Cdd:cd07584     5 IQMDSVLGDVKANLKKAAELCKEAAAEGADLICFPELATTGYRPDLLgPKLWELsEPIDGPTVRL--------------- 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1844083952 123 arLSCLAKDNSIYVLANLGDKKPCNSRdstcppngyfQYNTNVVYNTEGKLVARYHKV 180
Cdd:cd07584    70 --FSELAKELGVYIVCGFVEKGGVPGK----------VYNSAVVIDPEGESLGVYRKI 115

Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an essential membrane-bound enzyme in gram-negative bacteria, which catalyzes the N-acylation of apolipoproteins, the final step in lipoprotein maturation. This is a reverse amidase (i.e. condensation) reaction. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 9.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083952  34 AVILPNkteTPVSQEDALNLMNENIDILETAIKQAAEQGARIIVTPedalygwkftrETVFPYLEDIPDpqvnwipcqdp 113
Cdd:cd07571     4 ALVQGN---IPQDEKWDPEQRQATLDRYLDLTRELADEKPDLVVWP-----------ETALPFDLQRDP----------- 58

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083952 114 hrfghtPVQARLSCLAKDNSIYVLANLGDKKpcnsrdstcpPNGYFQYNTNVVYNTEGKLVARYHKV 180
Cdd:cd07571    59 ------DALARLARAARAVGAPLLTGAPRRE----------PGGGRYYNSALLLDPGGGILGRYDKH 109

Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1844083952  57 NIDILETAIKQAAEQGARIIVTPEDALYGWKFT-RETVFPYLEDIPD 102
Cdd:cd07580    17 NLARSIELIREAADAGANLVVLPELANTGYVFEsRDEAFALAEEVPD 63