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Database: UniProt
Entry: D9SF73_GALCS
LinkDB: D9SF73_GALCS
Original site: D9SF73_GALCS 
ID   D9SF73_GALCS            Unreviewed;       338 AA.
AC   D9SF73;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000313|EMBL:ADL55170.1};
DE            EC=2.5.1.54 {ECO:0000313|EMBL:ADL55170.1};
GN   OrderedLocusNames=Galf_1142 {ECO:0000313|EMBL:ADL55170.1};
OS   Gallionella capsiferriformans (strain ES-2) (Gallionella ferruginea
OS   capsiferriformans (strain ES-2)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Gallionellaceae; Gallionella.
OX   NCBI_TaxID=395494 {ECO:0000313|EMBL:ADL55170.1, ECO:0000313|Proteomes:UP000001235};
RN   [1] {ECO:0000313|EMBL:ADL55170.1, ECO:0000313|Proteomes:UP000001235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ES-2 {ECO:0000313|EMBL:ADL55170.1,
RC   ECO:0000313|Proteomes:UP000001235};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Davenport K.W., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA   Mikhailova N., Shelobolina E.S., Picardal F., Roden E., Emerson D.,
RA   Woyke T.;
RT   "Complete sequence of Gallionella capsiferriformans ES-2.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP002159; ADL55170.1; -; Genomic_DNA.
DR   RefSeq; WP_013293109.1; NC_014394.1.
DR   AlphaFoldDB; D9SF73; -.
DR   STRING; 395494.Galf_1142; -.
DR   KEGG; gca:Galf_1142; -.
DR   eggNOG; COG2876; Bacteria.
DR   HOGENOM; CLU_062599_0_0_4; -.
DR   OrthoDB; 9802281at2; -.
DR   Proteomes; UP000001235; Chromosome.
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:0009073; P:aromatic amino acid family biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR041071; DAHP_snth_FXD.
DR   InterPro; IPR006268; DAHP_syn_2.
DR   NCBIfam; TIGR01361; DAHP_synth_Bsub; 1.
DR   PANTHER; PTHR43018; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1.
DR   PANTHER; PTHR43018:SF2; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1.
DR   Pfam; PF18152; DAHP_snth_FXD; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001235};
KW   Transferase {ECO:0000313|EMBL:ADL55170.1}.
FT   DOMAIN          1..67
FT                   /note="DAHP synthase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF18152"
FT   DOMAIN          87..323
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   338 AA;  36832 MW;  72EC52B7F4AC4D36 CRC64;
     MIIVMGRDVT DEQIGTVVKR LETAGLKANI SRGIERTVIG AIGDERKLNE EMFTPLPGVE
     SAMHVTKQYK IVSRESHREN TIVDIGGVQL GGNQIQVIAG PCSVETQEQM DLSAKYVAEA
     GCRLMRGGAF KPRTSPYAFQ GHGAEGLDMF RKAASQYKLP IVTELMDARQ LDTFMEYDVD
     VIQIGTRNMQ NFDLLKEVGR INKPVILKRG MSATISEWLM AAEYIAAGGN HNIIFCERGI
     RTFETYYRNV LDVTAIPVLK KETHLPVIVD PSHAGGKAWM VAALSQAAIA AGADGLLVEM
     HPSPCDAWCD ADQALTPDEL KKLMGTLGAI AGAIGRTL
//
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