GLI_AGRFC
ID GLI_AGRFC Reviewed; 292 AA.
AC A9CEQ7;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=D-galactarolactone isomerase;
DE Short=GLI;
DE EC=5.4.1.4 {ECO:0000269|PubMed:24450804};
DE AltName: Full=Galactaro delta-lactone isomerase;
GN OrderedLocusNames=Atu3138;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP KINETIC PARAMETERS, PATHWAY, AND MUTAGENESIS OF ASN-240.
RC STRAIN=C58 / ATCC 33970;
RX PubMed=24450804; DOI=10.1021/bi5000492;
RA Bouvier J.T., Groninger-Poe F.P., Vetting M., Almo S.C., Gerlt J.A.;
RT "Galactaro delta-lactone isomerase: lactone isomerization by a member of
RT the amidohydrolase superfamily.";
RL Biochemistry 53:614-616(2014).
CC -!- FUNCTION: Catalyzes the isomerization of D-galactaro-1,5-lactone to D-
CC galactaro-1,4-lactone. This is a step in the oxidative degradation
CC pathway of D-galacturonate, which allows A.tumefaciens to utilize D-
CC galacturonate as a sole carbon source. {ECO:0000269|PubMed:24450804}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactaro-1,5-lactone = D-galactaro-1,4-lactone;
CC Xref=Rhea:RHEA:45580, ChEBI:CHEBI:83383, ChEBI:CHEBI:85317;
CC EC=5.4.1.4; Evidence={ECO:0000269|PubMed:24450804};
CC -!- COFACTOR:
CC Note=Does not require a metal cofactor. {ECO:0000269|PubMed:24450804};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.3 mM for D-galactaro-1,5-lactone {ECO:0000269|PubMed:24450804};
CC Note=kcat is 440 sec(-1).;
CC -!- PATHWAY: Carbohydrate acid metabolism; D-galacturonate degradation via
CC prokaryotic oxidative pathway. {ECO:0000269|PubMed:24450804}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC {ECO:0000305}.
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DR EMBL; AE007870; AAK90248.1; -; Genomic_DNA.
DR PIR; AD2942; AD2942.
DR PIR; F98340; F98340.
DR RefSeq; NP_357463.1; NC_003063.2.
DR RefSeq; WP_010972788.1; NC_003063.2.
DR PDB; 4MUP; X-ray; 1.60 A; A/B/C=1-292.
DR PDBsum; 4MUP; -.
DR AlphaFoldDB; A9CEQ7; -.
DR SMR; A9CEQ7; -.
DR STRING; 176299.Atu3138; -.
DR DNASU; 1140387; -.
DR EnsemblBacteria; AAK90248; AAK90248; Atu3138.
DR GeneID; 66223456; -.
DR KEGG; atu:Atu3138; -.
DR PATRIC; fig|176299.10.peg.2983; -.
DR eggNOG; COG3618; Bacteria.
DR HOGENOM; CLU_064039_2_1_5; -.
DR OMA; HTPRMKV; -.
DR PhylomeDB; A9CEQ7; -.
DR BioCyc; AGRO:ATU3138-MON; -.
DR BioCyc; MetaCyc:MON-19230; -.
DR BRENDA; 5.4.1.4; 200.
DR UniPathway; UPA01050; -.
DR Proteomes; UP000000813; Chromosome linear.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF04909; Amidohydro_2; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Reference proteome.
FT CHAIN 1..292
FT /note="D-galactarolactone isomerase"
FT /id="PRO_0000429432"
FT MUTAGEN 240
FT /note="N->D: 28-fold decrease in enzymatic activity. Does
FT not gain the ability to hydrolyze D-galactaro-1,5-lactone
FT or D-galactaro-1,4-lactone."
FT /evidence="ECO:0000269|PubMed:24450804"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:4MUP"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:4MUP"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:4MUP"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:4MUP"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:4MUP"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:4MUP"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:4MUP"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:4MUP"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:4MUP"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:4MUP"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:4MUP"
FT HELIX 132..141
FT /evidence="ECO:0007829|PDB:4MUP"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:4MUP"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:4MUP"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:4MUP"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:4MUP"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:4MUP"
FT HELIX 186..197
FT /evidence="ECO:0007829|PDB:4MUP"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:4MUP"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:4MUP"
FT HELIX 218..230
FT /evidence="ECO:0007829|PDB:4MUP"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:4MUP"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:4MUP"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:4MUP"
FT HELIX 255..263
FT /evidence="ECO:0007829|PDB:4MUP"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:4MUP"
FT HELIX 269..276
FT /evidence="ECO:0007829|PDB:4MUP"
FT HELIX 278..284
FT /evidence="ECO:0007829|PDB:4MUP"
SQ SEQUENCE 292 AA; 31983 MW; 4596112829F94E4B CRC64;
MSELVRKLSG TAPNPAFPRG AVDTQMHMYL PGYPALPGGP GLPPGALPGP EDYRRLMQWL
GIDRVIITQG NAHQRDNGNT LACVAEMGEA AHAVVIIDAT TTEKDMEKLT AAGTVGARIM
DLPGGAVNLS ELDAVDERAH AADWMVAVQF DGNGLLDHLP RLQKIRSRWV FDHHGKFFKG
IRTDGPEMAA LLKLIDRGNL WFKFAGVYES SRKSWPYADV AAFSRVIAAH APERIVWGTN
WPHNSVRETA AYPDDARLAE LTLGWLPDEA ARHRALVENP EALFKLSPVK AT
