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B6db families: bhcb

Activity bhcb
Description Erythro-3-hydroxy-D-aspartate ammonia-lyase (4.3.1.-)
Notes Bacterial sequences, very similar to eukaryotic serine racemases (family and to bacterial Threo-3-hydroxy-L-aspartate ammonia-lyases (family
At least one enzyme in family (from Pseudomonas sp. 99) also appears to catalyze quite efficiently the bhcB reaction.
PLP Fold Type II
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type II

Number of sequences 11
Sequences in seed alignment
BacteriaWP_012329919 (Methylobacterium radiotolerans); WP_065325298 (Epibacterium mobile); WP_007205928 (Yoonia vestfoldensis); WP_005864223 (Sagittula stellata); WP_011582621 (Chelativorans sp. BNC1); WP_007803858 (Salipiger bermudensis); WP_011455724 (Jannaschia sp. CCS1); WP_011280658 (Psychrobacter arcticus); WP_011241926 (Ruegeria pomeroyi); WP_041530430 (Paracoccus denitrificans DSM 413); WP_009812828 (Roseovarius nubinhibens);

DISPLAY: Fasta format, alignment, hmm, hmm_local

Reference sequence WP_041530430
Domain interval 20-308
Catalytic site 57 K
 Schada von Borzyskowski L, Severi F, Krüger K, Hermann L, Gilardet A, Sippel F, Pommerenke B, Claus P, Cortina NS, Glatter T, Zauner S, Zarzycki J, Fuchs BM, Bremer E, Maier UG, Amann RI, Erb TJ (2019) Marine Proteobacteria metabolize glycolate via the β-hydroxyaspartate cycle Nature 575 500-504.

 Nagano, H.; Shibano, K.; Matsumoto, Y.; Yokota, A.; Wada, M. (2017) Isolation and amino acid sequence of a dehydratase acting on d-erythro-3-hydroxyaspartate from Pseudomonas sp. N99, and its application in the production of optically active 3-hydroxyaspartate Biosci Biotechnol Biochem 81 1156-1164.

Articles on bhcb
last changed 2019/11/20 17:34

B6db families