ID G7LWS1_9GAMM Unreviewed; 474 AA.
AC G7LWS1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=pectate lyase {ECO:0000256|ARBA:ARBA00012272};
DE EC=4.2.2.2 {ECO:0000256|ARBA:ARBA00012272};
GN ORFNames=BrE312_1877 {ECO:0000313|EMBL:EHD21270.1};
OS Brenneria sp. EniD312.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Brenneria.
OX NCBI_TaxID=598467 {ECO:0000313|EMBL:EHD21270.1};
RN [1] {ECO:0000313|EMBL:EHD21270.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EniD312 {ECO:0000313|EMBL:EHD21270.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Monk A.C., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Balakrishnan V.,
RA Glasner J., Perna N., Woyke T.;
RT "Complete sequence of Brenneria sp. EniD312.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan to give
CC oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at
CC their non-reducing ends.; EC=4.2.2.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000695};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 3 family.
CC {ECO:0000256|ARBA:ARBA00006463}.
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; CM001230; EHD21270.1; -; Genomic_DNA.
DR RefSeq; WP_009112574.1; NZ_CM001230.1.
DR AlphaFoldDB; G7LWS1; -.
DR STRING; 598467.BrE312_1877; -.
DR eggNOG; COG5297; Bacteria.
DR HOGENOM; CLU_045645_0_0_6; -.
DR Proteomes; UP000002759; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030570; F:pectate lyase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR004898; Pectate_lyase_PlyH/PlyE-like.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR PANTHER; PTHR33407; PECTATE LYASE F-RELATED; 1.
DR PANTHER; PTHR33407:SF9; PECTATE LYASE F-RELATED; 1.
DR Pfam; PF03211; Pectate_lyase; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:EHD21270.1}.
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 46433 MW; B5B14F1CF5BAAAEA CRC64;
MADMTITLSI QPGAGLSSTG LNSPLSGSNS GGAPRSAQQD NQLMEALDTL LSALLPNSQG
NTPSSTDGSP LGQAGAGNGG SSALGQNGSP ADMLMKLLET LIQGKNGQEA GNPFASGSSG
ATGGNSGTSP LTGSSGTGDA GSAQNPEDLS RSLLQDSAGS ALDNAISPTA DGGGQLSTND
LLKALLELIG NLMDSQKGEF GQPQGSGQSQ GSGSPSVGVP QASSGGNGGS PTAPSAPSGG
ASPAAPSAPV GGSGGVSPGA SPAASTAGAG PVSFPTASGN ATVVNDTIKV GPGEVFDGGG
KTFTAGSKLG DGGQAEGQKP LFELAPGATL KNVVFGDNAA DGVHVRGDAK IDNVHWTNVG
EDALTVKSNG GKPANVEITN SSAQGASDKI FQLNADANLT IDNFKAKDFG TFVRTNGGQQ
GNWNLNLSNI DAENGKFSFV KSDSEGLNVK GSNINLTNVN NHYKVPDSAN LQVN
//
