ID   FDTA_ANETH              Reviewed;         139 AA.
AC   Q6T1W8;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   13-SEP-2023, entry version 60.
DE   RecName: Full=TDP-4-oxo-6-deoxy-alpha-D-glucose-3,4-oxoisomerase;
DE            EC=5.3.2.3;
DE   AltName: Full=dTDP-6-deoxy-3,4-keto-hexulose isomerase;
GN   Name=fdtA;
OS   Aneurinibacillus thermoaerophilus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC   Aneurinibacillus group; Aneurinibacillus.
OX   NCBI_TaxID=143495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=L420-91T;
RX   PubMed=12740380; DOI=10.1074/jbc.m300858200;
RA   Pfoestl A., Hofinger A., Kosma P., Messner P.;
RT   "Biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-D-galactose in
RT   Aneurinibacillus thermoaerophilus L420-91T.";
RL   J. Biol. Chem. 278:26410-26417(2003).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS), SUBUNIT, ACTIVE SITE, FUNCTION,
RP   CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-49 AND HIS-51.
RX   PubMed=17459872; DOI=10.1074/jbc.m702529200;
RA   Davis M.L., Thoden J.B., Holden H.M.;
RT   "The x-ray structure of dTDP-4-keto-6-deoxy-D-glucose-3,4-ketoisomerase.";
RL   J. Biol. Chem. 282:19227-19236(2007).
CC   -!- FUNCTION: Mediates the isomerization of dTDP-6-deoxy-D-xylohex-4-ulose
CC       into dTDP-6-deoxy-D-xylohex-3-ulose in the biosynthesis of dTDP-3-
CC       acetamido-3,6-dideoxy-alpha-D-galactose, a glycan chain of the S-layer.
CC       {ECO:0000269|PubMed:12740380, ECO:0000269|PubMed:17459872}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-3-dehydro-6-
CC         deoxy-alpha-D-galactose; Xref=Rhea:RHEA:31835, ChEBI:CHEBI:57649,
CC         ChEBI:CHEBI:63303; EC=5.3.2.3; Evidence={ECO:0000269|PubMed:12740380,
CC         ECO:0000269|PubMed:17459872};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17459872}.
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DR   EMBL; AY442352; AAS55720.1; -; Genomic_DNA.
DR   PDB; 2PA7; X-ray; 1.50 A; A/B=1-139.
DR   PDB; 2PAE; X-ray; 2.50 A; A/B=1-139.
DR   PDB; 2PAK; X-ray; 2.40 A; A/B=1-139.
DR   PDB; 2PAM; X-ray; 2.50 A; A/B=1-139.
DR   PDBsum; 2PA7; -.
DR   PDBsum; 2PAE; -.
DR   PDBsum; 2PAK; -.
DR   PDBsum; 2PAM; -.
DR   AlphaFoldDB; Q6T1W8; -.
DR   SMR; Q6T1W8; -.
DR   KEGG; ag:AAS55720; -.
DR   OrthoDB; 9795513at2; -.
DR   BioCyc; MetaCyc:MONOMER-17003; -.
DR   BRENDA; 5.3.2.3; 344.
DR   EvolutionaryTrace; Q6T1W8; -.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   CDD; cd20292; cupin_QdtA-like; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR008894; QdtA_cupin_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   Pfam; PF05523; FdtA; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Isomerase.
FT   CHAIN           1..139
FT                   /note="TDP-4-oxo-6-deoxy-alpha-D-glucose-3,4-oxoisomerase"
FT                   /id="PRO_0000421823"
FT   ACT_SITE        49
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000305|PubMed:17459872"
FT   MUTAGEN         49
FT                   /note="H->N: Loss of catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:17459872"
FT   MUTAGEN         51
FT                   /note="H->N: Retains some catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:17459872"
FT   STRAND          4..7
FT                   /evidence="ECO:0007829|PDB:2PA7"
FT   STRAND          10..13
FT                   /evidence="ECO:0007829|PDB:2PA7"
FT   STRAND          16..22
FT                   /evidence="ECO:0007829|PDB:2PA7"
FT   TURN            23..25
FT                   /evidence="ECO:0007829|PDB:2PA7"
FT   STRAND          26..29
FT                   /evidence="ECO:0007829|PDB:2PA7"
FT   STRAND          33..39
FT                   /evidence="ECO:0007829|PDB:2PA7"
FT   STRAND          46..53
FT                   /evidence="ECO:0007829|PDB:2PA7"
FT   STRAND          56..63
FT                   /evidence="ECO:0007829|PDB:2PA7"
FT   STRAND          65..70
FT                   /evidence="ECO:0007829|PDB:2PA7"
FT   STRAND          75..80
FT                   /evidence="ECO:0007829|PDB:2PA7"
FT   STRAND          85..89
FT                   /evidence="ECO:0007829|PDB:2PA7"
FT   STRAND          94..98
FT                   /evidence="ECO:0007829|PDB:2PA7"
FT   STRAND          105..112
FT                   /evidence="ECO:0007829|PDB:2PA7"
FT   HELIX           116..118
FT                   /evidence="ECO:0007829|PDB:2PA7"
FT   HELIX           123..135
FT                   /evidence="ECO:0007829|PDB:2PA7"
SQ   SEQUENCE   139 AA;  16042 MW;  EC32CB06F863F137 CRC64;
     MENKVINFKK IIDSRGSLVA IEENKNIPFS IKRVYYIFDT KGEEPRGFHA HKKLEQVLVC
     LNGSCRVILD DGNIIQEITL DSPAVGLYVG PAVWHEMHDF SSDCVMMVLA SDYYDETDYI
     RQYDNFKKYI AKINLEKEG
//