Adenylate forming domain, Class I superfamily; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 795118553  25 QVVKVFIVLTPQFLSRDKDQLTKELQQHVKSVTVSCKSPRKVEFILELLKTITGKIKQGELRKR 88
Cdd:cd05928  465 EVVKAFVVLAPQFLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 795118553  25 QVVKVFIVLTPQFLSRDKDQLTKELQQHVKSVTVSCKSPRKVEFILELLKTITGKIKQGELRKR 88
Cdd:cd05928  465 EVVKAFVVLAPQFLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528

benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 795118553   28 KVFIVLTPQFlsrdkDQLTKELQQHVKSVTVSCKSPRKVEFILELLKTITGKIKQGELRK 87
Cdd:TIGR02262 450 KAFVVLRPGQ-----TALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 795118553   25 QVVKVFIVLTPqflsrDKDQLTKELQQHVKSVTVSCKSPRKVEFILELLKTITGK 79
Cdd:pfam13193  27 EAPVAFVVLKP-----GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 795118553  25 QVVKVFIVLTPQFLSRDKDQLTKELQQHVKSVTVSCKSPRKVEFILELLKTITGKIKQGELRKR 88
Cdd:cd05928  465 EVVKAFVVLAPQFLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 795118553  25 QVVKVFIVLTPQFlsRDKDQLTKELQQHVKSVTVSCKSPRKVEFILELLKTITGKIKQGELRKR 88
Cdd:cd05970  475 QVVKATIVLAKGY--EPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRER 536

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795118553  25 QVVKVFIVLTPQFLsrDKDQLTKELQQHVKSVTVSCKSPRKVEFILELLKTITGKIKQGELR 86
Cdd:cd05971  379 EIVKAFVVLNPGET--PSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795118553  25 QVVKVFIVLTPQFLSrdKDQLTKELQQHVKSVTVSCKSPRKVEFILELLKTITGKIKQGELR 86
Cdd:cd05958  380 VVVKAFVVLRPGVIP--GPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 795118553  28 KVFIVLTPQFLSRDKdqLTKELQQHVKSVTVSCKSPRKVEFILELLKTITGKIKQGELR 86
Cdd:cd05919  380 TAFVVLKSPAAPQES--LARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436

benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 795118553   28 KVFIVLTPQFlsrdkDQLTKELQQHVKSVTVSCKSPRKVEFILELLKTITGKIKQGELRK 87
Cdd:TIGR02262 450 KAFVVLRPGQ-----TALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 795118553  25 QVVKVFIVLtpqflsRDKDQLTK-ELQQHVKSVTVSCKSPRKVEFILELLKTITGKIKQGELR 86
Cdd:cd05936  412 EAVKAFVVL------KEGASLTEeEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 795118553  25 QVVKVFIVLTPqflsrDKDQLTKELQQHVKSVTVSCKSPRKVEFILELLKTITGKIK 81
Cdd:cd04433  285 ERVVAVVVLRP-----GADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 795118553   25 QVVKVFIVLTPqflsrDKDQLTKELQQHVKSVTVSCKSPRKVEFILELLKTITGK 79
Cdd:pfam13193  27 EAPVAFVVLKP-----GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76

long-chain-fatty-acid--CoA ligase FadD;

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795118553  25 QVVKVFIVLTPQFLSRDkdqltkELQQHVKSVTVSCKSPRKVEFILELLKTITGKIKQGELR 86
Cdd:PRK08974 495 EAVKIFVVKKDPSLTEE------ELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550

Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 795118553  25 QVVKVFIVLTPQFLSRDKDQltkELQQHVKSVTVSCKSPRKVEFILELLKTITGKI 80
Cdd:cd05935  373 EEVKAFIVLRPEYRGKVTEE---DIIEWAREQMAAYKYPREVEFVDELPRSASGKI 425

long-chain fatty acid--CoA ligase;

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795118553  25 QVVKVFIVltpqflSRDKDQLTKELQQHVKSVTVSCKSPRKVEFILELLKTITGKIKQGELR 86
Cdd:PRK08751 500 EIVKVVIV------KKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 795118553  25 QVVKVFIVLTPQfLSRDKDQLTKELQQHVKSVTVSCKSPRKVEFILELLKTITGKIKQGELRK 87
Cdd:cd05967  534 QVPLGLVVLKEG-VKITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRK 595

long-chain-fatty-acid--CoA ligase; Validated

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 795118553  24 QQVVKVFIVLtpqflsRDKDQLT-KELQQHVKSVTVSCKSPRKVEFILELLKTITGKIKQGELRKR 88
Cdd:PRK06187 457 GERPVAVVVL------KPGATLDaKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQ 516

long-chain-fatty-acid--CoA ligase; Validated

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 795118553  43 DQLTKELQQHVKSVTVSCKSPRKVEFILELLKTITGKIKQGELRKR 88
Cdd:PRK08276 448 DALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDR 493

acyl-CoA synthetase; Validated

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 795118553  23 FQQVVKVFIVLTPQfLSRDKDqltkELQQHVKSVTVSCKSPRKVEFILELLKTITGKIKQGELRK 87
Cdd:PRK07788 488 FGQRLRAFVVKAPG-AALDED----AIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547