MHAA_STRAQ
ID MHAA_STRAQ Reviewed; 472 AA.
AC P80435; D6R238;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 3.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=3-hydroxy-4-methylanthranilate adenylyltransferase {ECO:0000305};
DE EC=2.7.7.97 {ECO:0000269|PubMed:10212227, ECO:0000269|PubMed:1318300};
DE AltName: Full=4-MHA-activating enzyme {ECO:0000305};
DE AltName: Full=4-methyl-3-hydroxyanthranilic acid-AMP ligase {ECO:0000303|PubMed:1318300};
DE Short=4-MHA-AMP ligase {ECO:0000303|PubMed:1318300};
DE AltName: Full=Actinomycin synthetase I {ECO:0000303|PubMed:1318300};
DE Short=ACMS I {ECO:0000303|PubMed:1318300};
GN Name=acmA {ECO:0000303|PubMed:9573200};
OS Streptomyces anulatus (Streptomyces chrysomallus).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1892;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-34.
RX PubMed=9573200; DOI=10.1128/jb.180.9.2468-2474.1998;
RA Schauwecker F., Pfennig F., Schroeder W., Keller U.;
RT "Molecular cloning of the actinomycin synthetase gene cluster from
RT Streptomyces chrysomallus and functional heterologous expression of the
RT gene encoding actinomycin synthetase II.";
RL J. Bacteriol. 180:2468-2474(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 11523 / DSM 40128 / JCM 4296 / LMG 20459 / NBRC 15393;
RX PubMed=10212227; DOI=10.1074/jbc.274.18.12508;
RA Pfennig F., Schauwecker F., Keller U.;
RT "Molecular characterization of the genes of actinomycin synthetase I and of
RT a 4-methyl-3-hydroxyanthranilic acid carrier protein involved in the
RT assembly of the acylpeptide chain of actinomycin in Streptomyces.";
RL J. Biol. Chem. 274:12508-12516(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 11523 / DSM 40128 / JCM 4296 / LMG 20459 / NBRC 15393;
RX PubMed=20304989; DOI=10.1128/jb.01526-09;
RA Keller U., Lang M., Crnovcic I., Pfennig F., Schauwecker F.;
RT "The actinomycin biosynthetic gene cluster of Streptomyces chrysomallus: a
RT genetic hall of mirrors for synthesis of a molecule with mirror symmetry.";
RL J. Bacteriol. 192:2583-2595(2010).
RN [4]
RP PROTEIN SEQUENCE OF 2-34.
RA Pahl A., Schlumbohm W., Keller U.;
RL Submitted (MAR-1995) to UniProtKB.
RN [5]
RP SEQUENCE REVISION TO 30.
RA Keller U.;
RL Submitted (NOV-1997) to UniProtKB.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=X2-18;
RX PubMed=1318300; DOI=10.1016/s0021-9258(19)49761-5;
RA Keller U., Schlumbohm W.;
RT "Purification and characterization of actinomycin synthetase I, a 4-methyl-
RT 3-hydroxyanthranilic acid-AMP ligase from Streptomyces chrysomallus.";
RL J. Biol. Chem. 267:11745-11752(1992).
CC -!- FUNCTION: Involved in the biosynthesis of actinomycin (PubMed:1318300).
CC Activates 4-methyl-3-hydroxyanthranilic acid (4-MHA), the precursor of
CC the chromophoric moiety of the actinomycin, as adenylate
CC (PubMed:1318300, PubMed:10212227). Can also use other benzene
CC carboxylic acids, such as 4-methyl-3-hydroxybenzoic acid (4-MHB) or 3-
CC hydroxyanthranilic acid (3-HA), but not pyridine, quinoline, or
CC quinoxaline carboxylic acids (PubMed:1318300).
CC {ECO:0000269|PubMed:10212227, ECO:0000269|PubMed:1318300}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxy-4-methylanthranilate + ATP + H(+) = 3-hydroxy-4-
CC methylanthranilyl-5'-AMP + diphosphate; Xref=Rhea:RHEA:24980,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:36558, ChEBI:CHEBI:91232; EC=2.7.7.97;
CC Evidence={ECO:0000269|PubMed:10212227, ECO:0000269|PubMed:1318300};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.4 uM for 4-MHA {ECO:0000269|PubMed:1318300};
CC KM=5 uM for 4-MHB {ECO:0000269|PubMed:1318300};
CC KM=18 uM for 3-HA {ECO:0000269|PubMed:1318300};
CC KM=110 uM for ATP {ECO:0000269|PubMed:1318300};
CC Note=kcat is 0.19 min(-1) with 4-MHA as substrate. kcat is 0.44 min(-
CC 1) with 4-MHB as substrate. kcat is 0.32 min(-1) with 3-HA as
CC substrate. {ECO:0000269|PubMed:1318300};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:10212227,
CC ECO:0000269|PubMed:1318300}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10212227}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; HM038106; ADG27357.1; -; Genomic_DNA.
DR RefSeq; WP_057667193.1; NZ_CM003601.1.
DR AlphaFoldDB; P80435; -.
DR SMR; P80435; -.
DR KEGG; ag:ADG27357; -.
DR PATRIC; fig|1892.7.peg.7097; -.
DR BioCyc; MetaCyc:MON-19510; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; ATP-binding; Cytoplasm; Direct protein sequencing;
KW Nucleotide-binding; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..472
FT /note="3-hydroxy-4-methylanthranilate adenylyltransferase"
FT /id="PRO_0000096467"
SQ SEQUENCE 472 AA; 51337 MW; E2A692EBD91725CC CRC64;
MADKWWGEQL LGRGDDGDLW AVSAAPVTRG ELRAGVAGLR LRFRESGISE GSSVLLRMTP
SFTYLQVLLA LWSCGAQVVL VDFRLKPAEF EPLVERVRPQ YLVVAAGAGG PVTGFRQESD
FEVRRLAGGR PAEDGVVLVQ FSSGSTGRPK VIGRPAGSVL AELDRHAGLP GTPGPGERVL
LLNSVMHNMG LMTGVLHALA AGATLVVPPT FRPAEVLRLM ARTEVSVMYG TPVHYDLLAR
TADRPERLSL RLAVSGGERV PEETRQRFLA AFGLPICQVY GVTEIGLIAG DLSGRCIPPE
IGPPVPGVEL EIDGEELLVR MDRSPYLYGE HTDRYRDGWL RTFDRVGRDP ETGVLSILGR
SDSLVVVGGL KVDLTEVEAA LLDHPRVAEV VVTHQDAIEA FVGGDEDLTA DELTAWCRER
LSAVKIPKRF FVTRQLPRNS MGKLARDRAL MHRHITSERS AQSRPAELKG AS
