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B6db Fold_types: 1

Fold type I

Main domain: 3 layers: a/b/a, mixed beta-sheet of 7 strands, order 3245671; strand 7 is antiparallel to the rest

Prototype sequence:
AATC_CHICK - Aspartate aminotransferase

Prototype structure:
PDB 1AAT;

PLP-dependent families with this fold:

1.17.1.1 (6) 1.4.4.2 (31) 2.1.2.1 (69) 2.1.2.7_a (8) 2.1.2.7_b (5) 2.2.1.8 (5) 2.3.1.29 (15) 2.3.1.37 (38) 2.3.1.47 (37) 2.3.1.50_a (14) 2.3.1.50_b (18) 2.3.1.50_c (18) 2.5.1.48_a (8) 2.5.1.48_b (10) 2.5.1.48_c (10) 2.5.1.49 (30) 2.5.1.73 (9) 2.6.1.100 (7) 2.6.1.102 (7) 2.6.1.103 (14) 2.6.1.104 (9) 2.6.1.105 (12) 2.6.1.106 (4) 2.6.1.108 (4) 2.6.1.109 (10) 2.6.1.11 (25) 2.6.1.110 (7) 2.6.1.111 (3) 2.6.1.112 (15) 2.6.1.113 (11) 2.6.1.115 (4) 2.6.1.117 (8) 2.6.1.118 (6) 2.6.1.13_a (34) 2.6.1.13_b (5) 2.6.1.17 (19) 2.6.1.18_a (17) 2.6.1.18_b (2) 2.6.1.19_a (14) 2.6.1.19_b (23) 2.6.1.1_a (40) 2.6.1.1_b (30) 2.6.1.1_c (11) 2.6.1.1_d (10) 2.6.1.1_e (13) 2.6.1.1_f (12) 2.6.1.27 (11) 2.6.1.28 (7) 2.6.1.29 (9) 2.6.1.2_a (30) 2.6.1.2_b (23) 2.6.1.2_c (14) 2.6.1.2_d (6) 2.6.1.30 (11) 2.6.1.33_a (2) 2.6.1.33_b (23) 2.6.1.34_a (11) 2.6.1.34_b (8) 2.6.1.36_a (15) 2.6.1.36_b (11) 2.6.1.37 (17) 2.6.1.39_a (17) 2.6.1.39_b (5) 2.6.1.39_c (8) 2.6.1.4 (10) 2.6.1.40 (19) 2.6.1.42_b (5) 2.6.1.44_a (30) 2.6.1.44_b (8) 2.6.1.45 (18) 2.6.1.50 (8) 2.6.1.52_a (42) 2.6.1.52_b (10) 2.6.1.55 (6) 2.6.1.57_a (14) 2.6.1.57_b (15) 2.6.1.57_c (18) 2.6.1.58 (2) 2.6.1.59 (5) 2.6.1.5_a (25) 2.6.1.5_b (5) 2.6.1.62 (30) 2.6.1.66_a (13) 2.6.1.66_b (19) 2.6.1.7 (24) 2.6.1.72 (7) 2.6.1.76 (30) 2.6.1.77 (14) 2.6.1.79 (9) 2.6.1.80 (11) 2.6.1.81 (7) 2.6.1.83_a (14) 2.6.1.83_b (4) 2.6.1.84 (3) 2.6.1.87 (9) 2.6.1.88_b (6) 2.6.1.89 (5) 2.6.1.9 (30) 2.6.1.90_a (11) 2.6.1.90_b (4) 2.6.1.92 (12) 2.6.1.93 (6) 2.6.1.94 (3) 2.6.1.96 (9) 2.6.1.98 (3) 2.8.1.7_a (41) 2.8.1.7_b (12) 2.8.1.7_c (10) 2.8.1.9 (8) 2.9.1.1 (28) 2.9.1.2 (20) 3.7.1.3 (27) 4.1.1.105_a (5) 4.1.1.105_b (3) 4.1.1.107 (12) 4.1.1.109_a (11) 4.1.1.109_b (9) 4.1.1.109_c (7) 4.1.1.11 (4) 4.1.1.12 (12) 4.1.1.14_a (7) 4.1.1.14_b (2) 4.1.1.15_a (22) 4.1.1.15_b (44) 4.1.1.17_2 (15) 4.1.1.18_b (15) 4.1.1.18_c (11) 4.1.1.18_e (3) 4.1.1.19_2 (10) 4.1.1.22_a (10) 4.1.1.22_b (11) 4.1.1.25_a (10) 4.1.1.25_b (12) 4.1.1.28 (41) 4.1.1.29 (11) 4.1.1.53 (5) 4.1.1.57 (10) 4.1.1.64 (12) 4.1.1.81 (9) 4.1.1.86 (14) 4.1.2.26 (6) 4.1.2.27 (35) 4.1.2.5 (41) 4.1.99.1 (16) 4.1.99.2 (18) 4.2.1.144 (8) 4.2.1.145 (3) 4.2.1.164 (6) 4.2.1.168 (5) 4.2.3.134 (10) 4.2.3.2 (17) 4.3.1.29 (16) 4.4.1.1 (34) 4.4.1.11 (32) 4.4.1.14_a (23) 4.4.1.14_b (5) 4.4.1.16_a (28) 4.4.1.16_b (12) 4.4.1.28_a (16) 4.4.1.28_c (8) 4.4.1.35_a (7) 4.4.1.35_b (5) 4.4.1.36 (21) 4.4.1.4 (7) 4.4.1.8_a (18) 4.4.1.8_b (9) 4.4.1.8_c (15) 4.4.1.8_d (3) 5.1.1.10 (7) 5.1.1.15 (10) 5.1.1.17 (4) 5.1.1.1_b (4) 5.1.1.21 (9) 5.4.3.8 (45) abarat4 (2) abmh (6) acmh (7) ala_decarboxylase (2) amine_transaminase (8) aniq (6) argm (3) asmd (1) asp-glu_1_decarboxylase (13) atms13 (2) bc5273 (11) besb (7) beta_transaminase (4) bhca (11) cap15 (4) ccbf (1) chdn (2) cndf (1) cobc (9) cqsa (12) crmg (4) cuab (5) dhap_transaminase (9) dhpd (3) dhph-n (3) dihydrorhizobitoxine_synthase (8) dmspaat (5) frbh (4) fum8 (3) fumi (2) gabt1 (10) genb1 (4) genb2 (2) gens2 (3) glii (4) hape (4) hisc (7) idnl3 (4) ind4 (2) kans2 (2) ktmb (9) l-lysine_2-aminotransferase_a (9) l-lysine_2-aminotransferase_b (3) l136 (4) lipk (9) lipo (9) lmbf (2) lnmj-sh (6) marg (5) mbnn (2) metser_aldolase (7) mety (4) mimosinase_a (4) mimosinase_b (3) mm260 (11) mocr (22) mppp (15) mur24 (5) mxcl (7) nikk (4) nysdii (9) o_succinylhomoserine_sulfhydrylase (12) obag (3) orf30 (3) ovob (12) oxyq (10) palb (8) papd (6) pctc (3) pctv (5) pgat (7) pigh (11) pks-atd (4) pqra (1) ptaa (10) pumg (4) pvdn (13) pydd (14) qbsb (2) redl (11) rubn4 (15) sant (3) serine_decarboxylase (14) sibq (6) smul_1544 (5) swb1 (4) sxta (3) temporary_his-at (5) temporary_x5p-at (5) thnj (2) tsra (4) uncharacterized_family_tt0402 (2) uncharacterized_family_yhfs (15) ustd (8) vas1 (10) vbsl (6) vzb9 (7) ywfg (7)

 Jansen RS, Mandyoli L, Hughes R, Wakabayashi S, Pinkham JT, Selbach B, Guinn KM, Rubin EJ, Sacchettini JC, Rhee KY (2020) Aspartate aminotransferase Rv3722c governs aspartate-dependent nitrogen metabolism in Mycobacterium tuberculosis Nat Commun 11 1960.

 Jansen RS, Mandyoli L, Hughes R, Wakabayashi S, Pinkham JT, Selbach B, Guinn KM, Rubin EJ, Sacchettini JC, Rhee KY (2020) Aspartate aminotransferase Rv3722c governs aspartate-dependent nitrogen metabolism in Mycobacterium tuberculosis Nat Commun 11 1960.

 Jansen RS, Mandyoli L, Hughes R, Wakabayashi S, Pinkham JT, Selbach B, Guinn KM, Rubin EJ, Sacchettini JC, Rhee KY (2020) Aspartate aminotransferase Rv3722c governs aspartate-dependent nitrogen metabolism in Mycobacterium tuberculosis Nat Commun 11 1960.

 Arciola JM, Horenstein NA. (2018) Characterization of the PLP-dependent transaminase initiating azasugar biosynthesis Biochem J 475 2241-2256.

 Chun SW, Hinze ME, Skiba MA, Narayan ARH (2018) Chemistry of a Unique Polyketide-like Synthase J Am Chem Soc. 140 2430-2433.

 Han X, Sun R, Sandalova T, Achour A. (2018) Structural and functional studies of Spr1654: an essential aminotransferase in teichoic acid biosynthesis in Streptococcus pneumoniae. Open Biology. 8 170248.

 Liechti G, Singh R, Rossi PL, Gray MD, Adams NE, Maurelli AT. (2018) Chlamydia trachomatis dapF Encodes a Bifunctional Enzyme Capable of Both d-Glutamate Racemase and Diaminopimelate Epimerase Activities MBio. 9 e00204-18.

 Naowarojna N, Huang P, Cai Y, Song H, Wu L, Cheng R, Li Y, Wang S, Lyu H, Zhang L, Zhou J, Liu P. (2018) In Vitro Reconstitution of the Remaining Steps in Ovothiol A Biosynthesis: C-S Lyase and Methyltransferase Reactions. Org Lett. 20 5427-5430.

 Park YJ, Kenney GE, Schachner LF, Kelleher NL, Rosenzweig AC. (2018) Repurposed HisC Aminotransferases Complete the Biosynthesis of Some Methanobactins. Biochemistry. 57 3515-3523.

 Ferla MP, Brewster JL, Hall KR, Evans GB, Patrick WM. (2017) Primordial-like enzymes from bacteria with reduced genomes. Molecular Microbiology. 105 508-524.

 Hasebe F, Matsuda K, Shiraishi T, Futamura Y, Nakano T, Tomita T, Ishigami K, Taka H, Mineki R, Fujimura T, Osada H, Kuzuyama T, Nishiyama M. (2016) Amino-group carrier-protein-mediated secondary metabolite biosynthesis in Streptomyces Nat Chem Biol. 12 967-972.

 Son HF, Kim KJ (2016) Structural Insights into a Novel Class of Aspartate Aminotransferase from Corynebacterium glutamicum PLoS One 11 e0158402.

 Ye Y, Minami A, Igarashi Y, Izumikawa M, Umemura M, Nagano N, Machida M, Kawahara T, Shin-Ya K, Gomi K, Oikawa H. (2016) Unveiling the Biosynthetic Pathway of the Ribosomally Synthesized and Post‐translationally Modified Peptide Ustiloxin B in Filamentous Fungi Angew Chem Int Ed Engl 55 8072-5.

 Muliandi A, Katsuyama Y, Sone K, Izumikawa M2, Moriya T, Hashimoto J, Kozone I, Takagi M, Shin-ya K, Ohnishi Y. (2014) Biosynthesis of the 4-methyloxazoline-containing nonribosomal peptides, JBIR-34 and -35, in Streptomyces sp. Sp080513GE-23 Chem Biol 21 923-34.

 Clark LF, Johnson JV, Horenstein NA (2011) Identification of a gene cluster that initiates azasugar biosynthesis in Bacillus amyloliquefaciens. Chembiochem 12 2147-50.

 Crnovcić I, Süssmuth R, Keller U. (2010) Aromatic C-methyltransferases with antipodal stereoselectivity for structurally diverse phenolic amino acids catalyze the methylation step in the biosynthesis of the actinomycin chromophore. Biochemistry. 49 9698-705.

 Heemstra JR Jr, Walsh CT, Sattely ES (2009) Enzymatic tailoring of ornithine in the biosynthesis of the Rhizobium cyclic trihydroxamate siderophore vicibactin J Am Chem Soc 13 15317-29.

 Mo S, Sydor PK, Corre C, Alhamadsheh MM, Stanley AE, Haynes SW, Song L, Reynolds KA, Challis GL (2008) Elucidation of the Streptomyces coelicolor pathway to 2-undecylpyrrole, a key intermediate in undecylprodiginine and streptorubin B biosynthesis Chem Biol. 15 137-48.

 Kaiser J.T.; Gromadski K.; Rother M.; Engelhardt H.; Rodnina M.V.; Wahl M.C. (2005) Structural and functional investigation of a putative archaeal selenocysteine synthase Biochemistry 44 13315-13327.

 Kuettner, E.; Hilgenfeld, R.; Weiss, M. S. (2002) The active principle of garlic at atomic resolution J Biol Chem 277 46402-7.

 Vogt RN, Spies HS, Steenkamp DJ. (2001) The biosynthesis of ovothiol A (N-methyl-4-mercaptohistidine). Identification of S-(4'-L-histidyl)-L-cysteine sulfoxide as an intermediate and the products of the sulfoxide lyase reaction. Eur J Biochem. 268 5229-41.

 McPhalen, C. A.; Vincent, M. G.; Jansonius, J. N. (1992) X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase J Mol Biol 225 495-517..

 Ford, G. C.; Eichele, G.; Jansonius, J. N. (1980) Three-dimensional structure of a pyridoxal-phosphate-dependent enzyme, mitochondrial aspartate aminotransferase Proc Natl Acad Sci U S A 77 2559-63..


B6db Fold_types