ID W0Z7U1_9MICO Unreviewed; 641 AA.
AC W0Z7U1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Anthranilate synthase component 1 {ECO:0000256|ARBA:ARBA00020653};
DE EC=4.1.3.27 {ECO:0000256|ARBA:ARBA00012266};
GN Name=phzB {ECO:0000313|EMBL:CDJ99446.1};
GN ORFNames=MIC448_150027 {ECO:0000313|EMBL:CDJ99446.1};
OS Microbacterium sp. C448.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1177594 {ECO:0000313|EMBL:CDJ99446.1, ECO:0000313|Proteomes:UP000028883};
RN [1] {ECO:0000313|EMBL:CDJ99446.1, ECO:0000313|Proteomes:UP000028883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C448 {ECO:0000313|EMBL:CDJ99446.1,
RC ECO:0000313|Proteomes:UP000028883};
RX PubMed=24526651; DOI=10.1128/genomeA.01113-13;
RA Martin-Laurent F., Marti R., Waglechner N., Wright G.D., Topp E.;
RT "Draft Genome Sequence of the Sulfonamide Antibiotic-Degrading
RT Microbacterium sp. Strain C448.";
RL Genome Announc. Announc.2:e01113-e01113(2014).
CC -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the two-
CC step biosynthesis of anthranilate, an intermediate in the biosynthesis
CC of L-tryptophan. In the first step, the glutamine-binding beta subunit
CC (TrpG) of anthranilate synthase (AS) provides the glutamine
CC amidotransferase activity which generates ammonia as a substrate that,
CC along with chorismate, is used in the second step, catalyzed by the
CC large alpha subunit of AS (TrpE) to produce anthranilate. In the
CC absence of TrpG, TrpE can synthesize anthranilate directly from
CC chorismate and high concentrations of ammonia.
CC {ECO:0000256|ARBA:ARBA00025634}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate +
CC pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58359; EC=4.1.3.27;
CC Evidence={ECO:0000256|ARBA:ARBA00000329};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5. {ECO:0000256|ARBA:ARBA00004873}.
CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a
CC beta subunit (TrpG) and a large alpha subunit (TrpE).
CC {ECO:0000256|ARBA:ARBA00011575}.
CC -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC {ECO:0000256|ARBA:ARBA00009562}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDJ99446.1}.
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DR EMBL; CBVQ010000057; CDJ99446.1; -; Genomic_DNA.
DR RefSeq; WP_036294897.1; NZ_HG779595.1.
DR AlphaFoldDB; W0Z7U1; -.
DR STRING; 1177594.MIC448_150027; -.
DR eggNOG; COG0147; Bacteria.
DR eggNOG; COG0512; Bacteria.
DR HOGENOM; CLU_028026_0_0_11; -.
DR OrthoDB; 8594609at2; -.
DR Proteomes; UP000028883; Unassembled WGS sequence.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.60.120.10; Anthranilate synthase; 1.
DR InterPro; IPR005801; ADC_synthase.
DR InterPro; IPR019999; Anth_synth_I-like.
DR InterPro; IPR015890; Chorismate_C.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR006221; TrpG/PapA_dom.
DR PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR PANTHER; PTHR11236:SF46; ANTHRANILATE SYNTHASE COMPONENT 1; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00096; GATASE.
DR SUPFAM; SSF56322; ADC synthase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Lyase {ECO:0000313|EMBL:CDJ99446.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028883}.
FT DOMAIN 125..382
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT DOMAIN 454..631
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 533
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 615
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 617
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 641 AA; 68842 MW; 8192C3A46A54FF3E CRC64;
MTGHRPPSDA DGSELLQRLR DSAEDRPLIL IARDGADVEV LTGTVVDVEL LADIPLVDAD
GSPQEVLALV PYRQVRERGF ECHDDGAPLR CIIVAERGTV SRDEAMRVLP ATPVPLHDTG
FDVSDEDYAE IVRDVIADEI GRGEGANFVI RRDFTARVDA DPRETALTWF RALLEHERGA
YWTFAIVTPG HVAVGASPEA HVSASGGVVT MNPISGTFRH PAGGSTPEAL AAFLENTKET
EELFMVVDEE LKMMSAVCSD GGRITGPHLK EMSRLTHTEY MLRGRSMLDP RDILRETMFA
PTVTGSPMQN ACTVIRRHET SARGYYSGVA ALFTPNGDAH DLDAPILIRT AYLVEGRLRV
PVGATLVRHS DPDGEVGETH GKAAGLLGAI GAVPRESAPA PVADPDAPTT PRAPLAEDPA
IATLLASRNS RLAPFWLNPQ DADAPGPFVG RSALVVDAED RFTTMLAHQL RHLGLTVRIA
HWSEVSDAEA SDAELLIAGP GPGDPLDDSP RMRRMREIVS ARLASGRPLL AVCLSHQILA
NTLGMTLAPL VRPHQGLQLS VDVFGKRPSI GFYNTFTVSV EPGTTRVGHT EIAADPVSGD
VYAMRGPGYA SVQGHLESIL SRDGIETLER LIAQAFAPVD A
//
