B6db families : 2_6_1

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2.6.1.62

Activity

2.6.1.62

Description

Adenosylmethionine--8-amino-7-oxononanoate aminotransferase

Notes

In the case of plant enzymes, which are bifunctional proteins containing also a N-terminal dethiobiotin synthetase domain, such domain has been removed from the sequences included in the family.

PDB

1QJ5;1QJ3;1DTY;3WY7;6ERK;

PLP Fold Type

PLP-dependent Domain

Domain alignment
Domain hmm

Fold type I

Number of sequences

Sequences in seed alignment

Bacteria	AAM71295 (Chlorobium tepidum); WP_011728881 (Mycobacterium smegmatis); BIOA_MYCTU (Mycobacterium tuberculosis); AAK89425 (Agrobacterium tumefaciens); CAE33824 (Bordetella bronchiseptica); BAC09487 (Thermosynechococcus elongatus ); WP_011512731 (Psychrobacter cryohalolentis); NP_230756 (Vibrio cholerae); BIOA_ERWHE (Erwinia herbicola); ZP_00044897 (Magnetococcus sp. MC-1); AAG47794 (Mesorhizobium loti); BIOA_SALTY (Salmonella typhimurium); NP_876017 (Prochlorococcus marinus); AAN49341 (Leptospira interrogans); NP_625533 (Streptomyces coelicolor ); BIOA_ECOLI (Escherichia coli); WP_078220262 (Acinetobacter pittii); BIOA_SERMA (Serratia marcescens); WP_078276723 (Moraxella caviae); BIOA_CORGL (Corynebacterium glutamicum); BIOA_HAEIN (Haemophilus influenzae);
Fungi	XP_451549 (Kluyveromyces lactis); BIOA_YEAST (Saccharomyces cerevisiae);
Viridiplantae	NP_200567 (Arabidopsis thaliana); XP_010913641 (Elaeis guineensis); XP_003610157 (Medicago truncatula); OAE18092 (Marchantia polymorpha); XP_016579645 (Capsicum annuum); XP_015579089 (Ricinus communis); BAK07223 (Hordeum vulgare);

DISPLAY: Fasta format, alignment, hmm, hmm_local

Reference sequence

BIOA_ECOLI

Domain interval

28-372

Catalytic site

274 K

References

Bezsudnova EY, Stekhanova TN, Popinako AV, Rakitina TV, Nikolaeva AY, Boyko KM, Popov VO (2018) Diaminopelargonic acid transaminase from Psychrobacter cryohalolentis is active towards (S)-(-)-1-phenylethylamine, aldehydes and α-diketones Appl Microbiol Biotechnol 102 71-80.

Fan S, Li DF, Wang DC, Fleming J, Zhang H, Zhou Y, Zhou L, Zhou J, Chen T, Chen G, Zhang XE, Bi L (2015) Structure and function of Mycobacterium smegmatis 7-keto-8-aminopelargonic acid (KAPA) synthase Int J Biochem Cell Biol 58 71-80.

Cobessi D, Dumas R, Pautre V, Meinguet C, Ferrer JL, Alban C (2012) Biochemical and structural characterization of the Arabidopsis bifunctional enzyme dethiobiotin synthetase-diaminopelargonic acid aminotransferase: evidence for substrate channeling in biotin synthesis Plant Cell 24 1608-25.

Bhor, V.M.; Dev, S.; Vasanthakumar, G.R.; Surolia, A. (2006) Spectral and kinetic characterization of 7,8-diaminopelargonic acid synthase from Mycobacterium tuberculosis IUBMB Life 58 225-33.

Mann S, Ploux O. (2006) 7,8-Diaminoperlargonic acid aminotransferase from Mycobacterium tuberculosis, a potential therapeutic target. Characterization and inhibition studies FEBS J 273 4778-89.

Eliot, A. C.; Sandmark, J.; Schneider, G.; Kirsch, J. F. (2002) The dual-specific active site of 7,8-diaminopelargonic acid synthase and the effect of the R391A mutation Biochemistry 41 12582-9.

Kack, H.; Sandmark, J.; Gibson, K.; Schneider, G.; Lindqvist, Y. (1999) Crystal structure of diaminopelargonic acid synthase: evolutionary relationships between pyridoxal-5'-phosphate-dependent enzymes J Mol Biol 291 857-76.

Articles on 2.6.1.62

last changed

2019/10/22 12:22