ID C5BNI5_TERTT Unreviewed; 697 AA.
AC C5BNI5;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=aminodeoxychorismate synthase {ECO:0000256|ARBA:ARBA00013139};
DE EC=2.6.1.85 {ECO:0000256|ARBA:ARBA00013139};
GN Name=pabAB {ECO:0000313|EMBL:ACR14600.1};
GN OrderedLocusNames=TERTU_2979 {ECO:0000313|EMBL:ACR14600.1};
OS Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Teredinibacter.
OX NCBI_TaxID=377629 {ECO:0000313|EMBL:ACR14600.1, ECO:0000313|Proteomes:UP000009080};
RN [1] {ECO:0000313|EMBL:ACR14600.1, ECO:0000313|Proteomes:UP000009080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39867 / T7901 {ECO:0000313|Proteomes:UP000009080};
RX PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT endosymbiont of marine wood-boring bivalves (shipworms).";
RL PLoS ONE 4:E6085-E6085(2009).
CC -!- SIMILARITY: In the C-terminal section; belongs to the anthranilate
CC synthase component I family. {ECO:0000256|ARBA:ARBA00005970}.
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DR EMBL; CP001614; ACR14600.1; -; Genomic_DNA.
DR AlphaFoldDB; C5BNI5; -.
DR STRING; 377629.TERTU_2979; -.
DR MEROPS; C26.959; -.
DR KEGG; ttu:TERTU_2979; -.
DR eggNOG; COG0147; Bacteria.
DR eggNOG; COG0512; Bacteria.
DR HOGENOM; CLU_006493_0_1_6; -.
DR Proteomes; UP000009080; Chromosome.
DR GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0009396; P:folic acid-containing compound 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; IPR005802; ADC_synth_comp_1.
DR InterPro; IPR005801; ADC_synthase.
DR InterPro; IPR019999; Anth_synth_I-like.
DR InterPro; IPR006805; Anth_synth_I_N.
DR InterPro; IPR015890; Chorismate_C.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR006221; TrpG/PapA_dom.
DR NCBIfam; TIGR00553; pabB; 1.
DR NCBIfam; TIGR00566; trpG_papA; 1.
DR PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR PANTHER; PTHR11236:SF18; AMINODEOXYCHORISMATE SYNTHASE; 1.
DR Pfam; PF04715; Anth_synt_I_N; 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 Aminotransferase {ECO:0000313|EMBL:ACR14600.1};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Lyase {ECO:0000313|EMBL:ACR14600.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009080};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACR14600.1}.
FT DOMAIN 4..185
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 241..371
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 429..683
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 169
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 171
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 697 AA; 76726 MW; 020EFE2135953CB3 CRC64;
MKTLLIDNFD SFTFNLYQLI AEVNGQPPTV VRNNAGDWDA LKTAGFDNIV ISPGPGRADS
EVDFGICAQV IREAQVPVLG VCLGHQGLCQ TMGGEVEYLR PVMHGRISQV FHQQDPLFGH
IPSPFAVVRY HSLVVSKVPS SLQVIAQTAD GANMAVRHRH RPMWGVQFHP ESVCTEYGRQ
LLVNFHNLTK AWYGPGFDAS AAASKPAKPA PVARSGRAPL KVFFRRLASC LQPSLFFKTC
FAASNTSFWL DSECFRSPQG RFSYMGDAAG PQAEILEYSQ QSQLLRVRTH EGESVVATPL
FSYLNEQLAE RELHNSELPF PFNLGYVGYL GYEMKGDCGY PVVHRADTPD ACLLFADRIC
VFDHQAQAIY LVCVDLEEEG DRAKQWLHQM EQHLAALSKI PVPDAPHAVD KHVAAANAQS
GLFVPAHTDQ AYLELIARAK EMLQRGESYE ICLTNQLSAP CEFEPLELFL RLRAENPAPY
ASYLCFDDLQ VVSCSPERFL TIDQCGRVET KPIKGTRRRA STAAADAQVI VELTENEKER
AENLMIVDLL RNDLGQVSKV GSVSVPALFT VETFETVHQM VSTVVSELEE ERTAVDCVRA
CFPGGSMTGA PKKRTLEILD QLEGRARGVY SGAIGYFALN GSADWSIVIR SLVCLQGRCS
LGVGGAITDL SDPRAELEET RIKAEAILRG VAGILGR
//
