FDTA_ANETH
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 03-AUG-2022, entry version 56.
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; Firmicutes; 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 BioCyc; MetaCyc:MON-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; -; 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; SSF51182; 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
