ID B7N0R9_ECO81 Unreviewed; 523 AA.
AC B7N0R9;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Galactarate dehydratase (L-threo-forming) {ECO:0000256|HAMAP-Rule:MF_02031};
DE Short=GalcD {ECO:0000256|HAMAP-Rule:MF_02031};
DE EC=4.2.1.42 {ECO:0000256|HAMAP-Rule:MF_02031};
GN Name=garD {ECO:0000256|HAMAP-Rule:MF_02031,
GN ECO:0000313|EMBL:CAR09937.2};
GN OrderedLocusNames=ECED1_3790 {ECO:0000313|EMBL:CAR09937.2};
OS Escherichia coli O81 (strain ED1a).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585397 {ECO:0000313|EMBL:CAR09937.2, ECO:0000313|Proteomes:UP000000748};
RN [1] {ECO:0000313|Proteomes:UP000000748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ED1a {ECO:0000313|Proteomes:UP000000748};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- FUNCTION: Catalyzes the dehydration of galactarate to form 5-dehydro-4-
CC deoxy-D-glucarate (5-KDG). {ECO:0000256|HAMAP-Rule:MF_02031}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=galactarate = 5-dehydro-4-deoxy-D-glucarate + H2O;
CC Xref=Rhea:RHEA:16005, ChEBI:CHEBI:15377, ChEBI:CHEBI:16537,
CC ChEBI:CHEBI:42819; EC=4.2.1.42; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_02031};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02031};
CC -!- PATHWAY: Carbohydrate acid metabolism; galactarate degradation; D-
CC glycerate from galactarate: step 1/3. {ECO:0000256|HAMAP-
CC Rule:MF_02031}.
CC -!- SIMILARITY: Belongs to the UxaA family. {ECO:0000256|ARBA:ARBA00010986,
CC ECO:0000256|HAMAP-Rule:MF_02031}.
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DR EMBL; CU928162; CAR09937.2; -; Genomic_DNA.
DR RefSeq; WP_001273939.1; NC_011745.1.
DR AlphaFoldDB; B7N0R9; -.
DR KEGG; ecq:ECED1_3790; -.
DR HOGENOM; CLU_029189_0_0_6; -.
DR UniPathway; UPA00565; UER00629.
DR Proteomes; UP000000748; Chromosome.
DR GO; GO:0008867; F:galactarate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046392; P:galactarate catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd11613; SAF_AH_GD; 1.
DR Gene3D; 2.30.130.110; -; 1.
DR HAMAP; MF_02031; Galactar_dehydrat; 1.
DR InterPro; IPR017654; GarD-like.
DR InterPro; IPR032893; GarD_Enterobacteriaceae.
DR InterPro; IPR048332; GD_AH_C.
DR InterPro; IPR007392; GD_AH_second.
DR InterPro; IPR013974; SAF.
DR InterPro; IPR044144; UxaA/GarD_SAF.
DR NCBIfam; TIGR03248; galactar-dH20; 1.
DR PANTHER; PTHR30536; ALTRONATE/GALACTARATE DEHYDRATASE; 1.
DR PANTHER; PTHR30536:SF1; GALACTARATE DEHYDRATASE (L-THREO-FORMING); 1.
DR Pfam; PF20629; GD_AH_C; 1.
DR Pfam; PF04295; GD_AH_second; 1.
DR Pfam; PF08666; SAF; 1.
DR SMART; SM00858; SAF; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|HAMAP-Rule:MF_02031};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02031};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02031}.
FT DOMAIN 22..92
FT /note="SAF"
FT /evidence="ECO:0000259|SMART:SM00858"
SQ SEQUENCE 523 AA; 56334 MW; 8B1DC24245311C97 CRC64;
MANIKIRQET PTAFYIKVHD TDNVAIIVND NGLKAGTRFP DGLELIEHIP QGHKVALLDI
PANGEIIRYG EVIGYAVRAI PRGSWIDESM VVLPEAPPLH TLPLATKVPE PLPPLEGYTF
EGYRNADGSV GTKNLLGITT SVHCVAGVVD YVVKIIERDL LPKYPNVDGV VGLNHLYGCG
VAINAPAAVV PIRTIHNISL NPNFGGEVMV IGLGCEKLQP ERLLTGTDDV QAIPVESASI
VSLQDEKHVG FQSMVEDILQ VAECHLQKLN QRQRETCPAS ELVVGMQCGG SDAFSGVTAN
PAVGYASDLL VRCGATVMFS EVTEVRDAIH LLTPRAVNEE VGKRLLEEME WYDNYLNMGK
TDRSANPSPG NKKGGLANVV EKALGSIAKS GKSAIVEVLS PGQRPTKRGL IYAATPASDF
VCGTQQVASG ITVQVFTTGR GTPYGLMAVP VIKMATRTEL ANRWFDLMDI NAGTIATGEE
TIEEVGWKLF HFILDVASGK KKTFSDQWGL HNQLAVFNPA PVT
//
