KEGG   ENZYME: 2.7.7.97
Entry
EC 2.7.7.97                 Enzyme                                 
Name
3-hydroxy-4-methylanthranilate adenylyltransferase;
acmA (gene name);
sibE (gene name);
actinomycin synthase I;
4-MHA-activating enzyme;
ACMS I;
actinomycin synthetase I;
4-MHA pentapeptide lactone synthase AcmA
Class
Transferases;
Transferring phosphorus-containing groups;
Nucleotidyltransferases
Sysname
ATP:3-hydroxy-4-methylanthranilate adenylyltransferase
Reaction(IUBMB)
ATP + 3-hydroxy-4-methylanthranilate = diphosphate + 3-hydroxy-4-methylanthranilyl-adenylate [RN:R11554]
Reaction(KEGG)
R11554
Substrate
ATP [CPD:C00002];
3-hydroxy-4-methylanthranilate [CPD:C03986]
Product
diphosphate [CPD:C00013];
3-hydroxy-4-methylanthranilyl-adenylate
Comment
The enzyme, characterized from the bacteria Streptomyces anulatus and Streptosporangium sibiricum, activates 3-hydroxy-4-methylanthranilate, a precursor of actinomycin antibiotics and the antitumor antibiotic sibiromycin, to an adenylate form, so it can be loaded onto a dedicated aryl-carrier protein.
History
EC 2.7.7.97 created 2016
Orthology
K21284  3-hydroxy-4-methylanthranilate adenylyltransferase
Genes
KGRJJJ10_13575
KLMBWI76_15080
VRURND59_08015
PCELHUB94_18035
NBRO3I_021160
NOZDMB37_35945
NHUH0264_30690
SANLKZO11_29675
SGRFSGFS_035550 SGFS_087230
SCBSCAB_69851
SRCM271_02960
SBHSBI_01606
SLDT261_0691 T261_2098
SPAVSpa2297_02690 Spa2297_26635
SPHWNFX46_21455
SLSSLINC_4426 SLINC_6767
SPLULK06_031595
SGVB1H19_08420
SFKKY5_6714 KY5_6734
SDXC4B68_39065
SKACP970_06985 CP970_07075
SBYH7H31_03490
SFEUIM697_30790
SAUHSU9_026730
SLFJEQ17_24455
SDECL3078_11315
SRUGF0345_28460
SAKBK1J60_34225
SCAEIHE65_34330
SANTQR300_02495
SYUNMOV08_33800
SJNRI060_03955
SHAUK9S39_40180
SKGKJK29_03005
SCOAQU709_20155 QU709_24610
SLAIP8A22_34825
STRZOYE22_03360
KSKKSE_65160 KSE_67410
KISHUT16_30905 HUT16_31040 HUT16_31825
STRIC7M71_007290
STRHGXP74_15530 GXP74_26115
ABRYNYE86_02840
RTXTI83_07420
RTCAPU90_09660
MPORKW076_03645
CXIENP048_18850
KFLKfla_6074
KSLOG809_05965
NAKEKGD83_15170
AROONQK81_43525
SESPBN6_21380 BN6_63880
SSYIEKG83_30965 EKG83_36315
KALKALB_2251
KUTJJ691_50990
KPHYAOZ06_26445
AHMTL08_06700
ACTIUA75_06460
ACADUA74_06460
AHGAHOG_06230(lcfB1)
ALOCRK56726
ACTUActkin_05211(bclA_2)
UMERM788_01320 RM788_07320
STPStrop_2497
SAQSare_2681
MAUMicau_3489
MILML5_4902
MICBMicB006_2544
MTUACSH63_07600
MICHFJK98_16405
MTEMGCE86_13445
MCABHXZ27_18170
MSAGGCM10017556_53700
MCHLPVK74_07690
MFEUH1D33_23030
MHAWRMN56_24410
ACTNL083_2872
PFLAPflav_007540
PSUUPsuf_064580
CATICS0771_77100
DVCDvina_13840 Dvina_29170
DFUDfulv_12485
DAURDaura_12975
DMATDmats_13375 Dmats_24410
CAICaci_3250
 » show all
Reference
1  [PMID:10212227]
  Authors
Pfennig F, Schauwecker F, Keller U
  Title
Molecular characterization of the genes of actinomycin synthetase I and of a 4-methyl-3-hydroxyanthranilic acid carrier protein involved in the assembly of the acylpeptide chain of actinomycin in Streptomyces.
  Journal
J Biol Chem 274:12508-16 (1999)
DOI:10.1074/jbc.274.18.12508
  Sequence
Reference
2  [PMID:21612226]
  Authors
Giessen TW, Kraas FI, Marahiel MA
  Title
A four-enzyme pathway for 3,5-dihydroxy-4-methylanthranilic acid formation and incorporation into the antitumor antibiotic sibiromycin.
  Journal
Biochemistry 50:5680-92 (2011)
DOI:10.1021/bi2006114
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 2.7.7.97
IUBMB Enzyme Nomenclature: 2.7.7.97
ExPASy - ENZYME nomenclature database: 2.7.7.97
BRENDA, the Enzyme Database: 2.7.7.97

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