B6db families : arg

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arg aminomutase

Activity

Description

Arginine 2,3-aminomutase (5.4.3.-)

Notes

Arginine-2,3-aminomutase should require a [4Fe-4S] cluster, S-adenosyl-L-methionine (SAM), and pyridoxal-5'-phosphate as cofactors.

The sequence in this family are most similar to L-Lysine aminomutases (5.4.3.2); the prototype enzyme (from S. griseochromogenes) is also substantially active towards L-lysine.

PLP Fold Type

VII

PLP-dependent Domain

Domain alignment
Domain hmm

Fold type VII

Number of sequences

Sequences in seed alignment

Bacteria

AAP03121 (Streptomyces griseochromogenes); KUH39769 (Streptomyces kanasensis); WP_00634843 (Streptomyces tsukubensis); WP_020556026 (Streptomyces scabrisporus); PHQ52736 (Streptomyces cinnamoneus); WP_079101383 (Streptomyces pathocidini); WP_086571596 (Streptomyces alboverticillatus); WP_085923133 (Streptomyces platensis); SER97293 (Streptomyces qinglanensis); WP_093858595. (Streptomyces sp. TLI_053);

DISPLAY: Fasta format, alignment, hmm, hmm_local

Reference sequence

AAP03121

Domain interval

128-289

Catalytic site

348 K

References

Zhao J, Ji W, Ji X, Zhang Q (2020) Biochemical Characterization of an Arginine 2,3‐aminomutase with Dual Substrate Specificity Chin. J. Chem. 38 in press.

Cone MC, Yin X, Grochowski LL, Parker MR, Zabriskie TM. (2003) The blasticidin S biosynthesis gene cluster from Streptomyces griseochromogenes: sequence analysis, organization, and initial characterization Chembiochem 4 821-8.

Prabhakaran P. C., Woo N-T., Yorgey P.S., Gould S.J. (1988) Biosynthesis of blasticidin S from L-alpha-arginine. Stereochemistry in the arginine-2,3-aminomutase reaction J. Am. Chem. Soc. 110 5785-91.

Articles on arg.aminomutase

last changed

2020/04/23 09:13