ID A0A164CGA8_9MICO Unreviewed; 613 AA.
AC A0A164CGA8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Anthranilate synthase component 1 {ECO:0000256|ARBA:ARBA00020653};
DE EC=4.1.3.27 {ECO:0000256|ARBA:ARBA00012266};
GN Name=pabA {ECO:0000313|EMBL:KZE91729.1};
GN ORFNames=AVP41_01275 {ECO:0000313|EMBL:KZE91729.1};
OS Microbacterium sp. TNHR37B.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1775956 {ECO:0000313|EMBL:KZE91729.1, ECO:0000313|Proteomes:UP000076535};
RN [1] {ECO:0000313|EMBL:KZE91729.1, ECO:0000313|Proteomes:UP000076535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TNHR37B {ECO:0000313|EMBL:KZE91729.1,
RC ECO:0000313|Proteomes:UP000076535};
RA Adelskov J., Patel B.K.;
RT "Draft Genome Sequence of Microbacterium sp. TNHR37B isolated from the
RT Great Artesian Basin of Australia.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:KZE91729.1}.
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DR EMBL; LQGV01000001; KZE91729.1; -; Genomic_DNA.
DR RefSeq; WP_067162199.1; NZ_LQGV01000001.1.
DR AlphaFoldDB; A0A164CGA8; -.
DR STRING; 1775956.AVP41_01275; -.
DR PATRIC; fig|1775956.3.peg.1260; -.
DR Proteomes; UP000076535; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; PR00097; ANTSNTHASEII.
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 Reference proteome {ECO:0000313|Proteomes:UP000076535}.
FT DOMAIN 104..362
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT DOMAIN 417..593
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 497
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 577
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 579
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 613 AA; 67889 MW; EA73B33B6AF81F58 CRC64;
MFDLAAEAFA LVMKDGQVHQ FAGDSMLFDD LDQARSHPGE KIVAIPFRQA LWGDRPMSAA
ERRARQHVSS IQVHHHEKTP LRDFLAQADL ESVELRSGHF DVNDQEYAER VRAVIDNEIR
AGHGSNFVLH RTYQGRVDKR DPSIELSIFH ALLRKQVGAY WTFLVHFPDH TLIGASPEMH
LSRTEDGLTT MNPISGTYRY PSGGPDAASL REFLQDPKER NELYMVVDEE LKIMADLCEE
RPWVSGPQLR FMSNLAHTEY FIHGYSSLDW ATVIRRSLIA PTILGSPLES AFRMAARNDL
SPRGYLGGVL AHVSGKDTGD FDSAILIRTA CLEQTGEVSI PVGSTIVRDS DPVVEAAETS
AKVSTVLTGF SRKGDDDALA TLGREFLEGR RSEVADFWNQ EVREWYQGML PSPRRALVVD
HEDRFTGMLA AHLRSMGLDV QVVTGYPTES ELASADLLVL GPGPGDPNDD NDPRIANARS
LARRVVAERR VPTLAVCLSH QVVCRELGFE VRRLALPNQG TQRNIQVFGE EVRVGFYNSF
CAFGHADIDS VVDVASDSRT GEVHAIRTDN LIGFQFHPES ILSVDGARVL RSAVETLLTN
STATAMAATQ SST
//
