ID V2YB73_9FIRM Unreviewed; 337 AA.
AC V2YB73;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000313|EMBL:ESL12852.1};
DE EC=2.5.1.54 {ECO:0000313|EMBL:USF28448.1};
GN Name=aroF {ECO:0000313|EMBL:USF28448.1};
GN ORFNames=N510_003409 {ECO:0000313|EMBL:USF28448.1}, N510_02912
GN {ECO:0000313|EMBL:ESL12852.1};
OS Firmicutes bacterium ASF500.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1378168 {ECO:0000313|EMBL:ESL12852.1};
RN [1] {ECO:0000313|EMBL:ESL12852.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF500 {ECO:0000313|EMBL:ESL12852.1};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
RN [2] {ECO:0000313|EMBL:USF28448.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF500 {ECO:0000313|EMBL:USF28448.1};
RA Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT Model to Study Microbiome Function.";
RL Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AYJP01000018; ESL12852.1; -; Genomic_DNA.
DR EMBL; CP097573; USF28448.1; -; Genomic_DNA.
DR AlphaFoldDB; V2YB73; -.
DR STRING; 1378168.N510_02912; -.
DR PATRIC; fig|1378168.3.peg.3039; -.
DR eggNOG; COG2876; Bacteria.
DR HOGENOM; CLU_062599_0_0_9; -.
DR OrthoDB; 9780456at2; -.
DR Proteomes; UP000017395; Chromosome.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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:SF3; CARBOXYSOME FORMATION PROTEIN; 1.
DR PANTHER; PTHR43018; 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:UP000017395};
KW Transferase {ECO:0000313|EMBL:USF28448.1}.
FT DOMAIN 1..67
FT /note="DAHP synthase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18152"
FT DOMAIN 87..325
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 337 AA; 36479 MW; 29DD5369402C19F2 CRC64;
MIVILKPNHN PDQLNSLVSW LQEKGITIHT SIGEANTVLG LVGDTSTLDT DLIAALDIVE
DVKRVQEPYK NANRKFHPED TVIQVGSTQI GGGTLTIMAG PCSVESEDQV VAIAKAVKAS
GATMLRGGAF KPRTSPYAFQ GLGERGLEYL KAARAETGLP IVTELMDLSH LPLFKDVDVI
QIGARNMQNF DLLKAVGHQD KPVMIKRGMS ATYEEWLMSA EYVMAGGNEN VILCERGIRT
FESYTRNTLD LAAIPVLRRM THLPVIVDPS HATGKYWLVE PLAMGAVAIG ADGLQIEVHN
DPAHALCDGP QSLKPEAFDP LAKKLLALHS ALRGMEG
//
