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Database: UniProt
Entry: A0A3A4B0F3_9ACTN
LinkDB: A0A3A4B0F3_9ACTN
Original site: A0A3A4B0F3_9ACTN 
ID   A0A3A4B0F3_9ACTN        Unreviewed;      1035 AA.
AC   A0A3A4B0F3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   05-FEB-2025, entry version 19.
DE   SubName: Full=3-deoxy-7-phosphoheptulonate synthase {ECO:0000313|EMBL:RJL34329.1};
DE            EC=2.5.1.54 {ECO:0000313|EMBL:RJL34329.1};
GN   Name=aroF {ECO:0000313|EMBL:RJL34329.1};
GN   ORFNames=D5H75_07740 {ECO:0000313|EMBL:RJL34329.1};
OS   Bailinhaonella thermotolerans.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Bailinhaonella.
OX   NCBI_TaxID=1070861 {ECO:0000313|EMBL:RJL34329.1, ECO:0000313|Proteomes:UP000265768};
RN   [1] {ECO:0000313|EMBL:RJL34329.1, ECO:0000313|Proteomes:UP000265768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 75507 {ECO:0000313|EMBL:RJL34329.1,
RC   ECO:0000313|Proteomes:UP000265768};
RA   Tang S., Feng Y.;
RT   "YIM 75507 draft genome.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:RJL34329.1}.
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DR   EMBL; QZEY01000002; RJL34329.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A4B0F3; -.
DR   OrthoDB; 24041at2; -.
DR   Proteomes; UP000265768; Unassembled WGS sequence.
DR   GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:InterPro.
DR   CDD; cd01561; CBS_like; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR041472; BL00235/CARNS1_N.
DR   InterPro; IPR052899; Class-I_DAHP_synthase.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR006268; DAHP_syn_2.
DR   InterPro; IPR040570; LAL_C2.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR01361; DAHP_synth_Bsub; 1.
DR   PANTHER; PTHR43018; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1.
DR   PANTHER; PTHR43018:SF1; PROTEIN AROA(G); 1.
DR   Pfam; PF13535; ATP-grasp_4; 1.
DR   Pfam; PF18130; ATPgrasp_N; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   Pfam; PF18603; LAL_C2; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265768};
KW   Transferase {ECO:0000313|EMBL:RJL34329.1}.
FT   DOMAIN          455..654
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   1035 AA;  109115 MW;  26FFC0EF36CE2570 CRC64;
     MLSNSLIEVI GGTPLVRLRA GAARGVEVYA KLEMQNPFAM KDRVAKQIIT RARETGALAE
     GAPIVESSSG TMALGVALVG TLLGHPVHIV TDPRIDRITL AKLTGLGCEV HVVPRMDEHG
     WQGARLTRLD ELMNELPGAF WPRQYANPEN PAAYRALAGE LAADLEDIDT IVGSVGSGGS
     LCGTARALRE RLPGVTVVGV DCVGSVLFGQ PDRPRRLQSG LGNSLVPPNL DHSLIDEVHW
     LNDREAFEAT RALAREEKLF AGNTSGSVYR VLTWLAGRAE PGTRIVGIFP DRGDRYAETA
     HSEEYWAERG LGDLPLARAP KRVTPGTAVS SWSYRVEESG RPPLFVFVES NTTGSGMRAL
     TAARDLGYRA VLATGRPERY RGLDATGAAV VTCDTNDHRA LREAVTAAAG RDVVAAVSTT
     SEFYLIAAAR LAAELGLPAA DAGAVGRCRD KSLLRETLAA AGVRQPEHRV VTGPDAAREA
     AAAVGLPCVV KPVDDSGSTN VLRCESAGDA AAQAERILAV TRNVRGQATR RAVLVERLLD
     QPEYSVEMFG AGGEQRLLGI VEKTVTPGPH FVETRHILPA DLPAEAAAEM TATVRDALAA
     VSLESGPSHT EVKLGPDGAS IVEINPRLAG GMIPELFRLV TGADLLEAQV RFAAGREPGL
     PESFDGYAGI QFLLPAEAGV LAEVTGADLA AALPGVRSVT VTVEPGDRVA PPTDAYGRAG
     HVIATAPTRA ELAATLDRAA ALVEFRVRRE PASPYPLVSR AARDDRSVVE VGGVSIGPDT
     FTLIAGPCAV ETPEQTLAAA RLARAAGASL LRGGAFKPRS SPYGFRGLRA EALRILAEVR
     AETGLPVVTE VVDSRDVDLV ADWADMLQVG TRNMQNFGLL EAVGDSGRPV LLKRGMSATI
     EEWLLAAEYI ASRGNEAIVL CERGIRTFEP ATRNTLDLSA VLVAQGLSHL PVVVDPSHAA
     GRRDLVVPLA RAAVAAGADG VMIDVHPSPA DALCDGPQAL GERELSELPG AIRDWATLAG
     RLPREVLAPE SAALR
//
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