ID A0A0A6UV64_ACTUT Unreviewed; 267 AA.
AC A0A0A6UV64;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Pectate lyase {ECO:0000256|ARBA:ARBA00012272, ECO:0000256|RuleBase:RU367009};
DE EC=4.2.2.2 {ECO:0000256|ARBA:ARBA00012272, ECO:0000256|RuleBase:RU367009};
GN ORFNames=MB27_05570 {ECO:0000313|EMBL:KHD78309.1};
OS Actinoplanes utahensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1869 {ECO:0000313|EMBL:KHD78309.1, ECO:0000313|Proteomes:UP000054537};
RN [1] {ECO:0000313|EMBL:KHD78309.1, ECO:0000313|Proteomes:UP000054537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 12052 {ECO:0000313|EMBL:KHD78309.1,
RC ECO:0000313|Proteomes:UP000054537};
RA Velasco-Bucheli B., del Cerro C., Hormigo D., Garcia J.L., Acebal C.,
RA Arroyo M., de la Mata I.;
RT "Draft genome sequence of Actinoplanes utahensis NRRL 12052.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the depolymerization of both polygalacturonate and
CC pectins of methyl esterification degree from 22 to 89%, with an endo
CC mode of action. In contrast to the majority of pectate lyases, displays
CC high activity on highly methylated pectins.
CC {ECO:0000256|RuleBase:RU367009}.
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 ECO:0000256|RuleBase:RU367009};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913,
CC ECO:0000256|RuleBase:RU367009};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU367009}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 3 family.
CC {ECO:0000256|ARBA:ARBA00006463, ECO:0000256|RuleBase:RU367009}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHD78309.1}.
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DR EMBL; JRTT01000005; KHD78309.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A6UV64; -.
DR STRING; 1869.MB27_05570; -.
DR eggNOG; COG5297; Bacteria.
DR Proteomes; UP000054537; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030570; F:pectate lyase activity; IEA:UniProtKB-UniRule.
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 Calcium {ECO:0000256|RuleBase:RU367009};
KW Lyase {ECO:0000256|RuleBase:RU367009, ECO:0000313|EMBL:KHD78309.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054537};
KW Secreted {ECO:0000256|RuleBase:RU367009}.
SQ SEQUENCE 267 AA; 27195 MW; B4C55F010942C183 CRC64;
MFNNLRKRWR AGIVAVAAVG LGLGAVVYTQ GASAAAWPTA TGSVKLTASK AVSGTLDGGL
KRYVGSGALG GSGQDEGQDP LFVLADGATL KNVIIGSPAA DGVHCLGSCT ISNVWWENVG
EDAATFKGGN SAKYTVTGGA AKGADDKVFQ HNGGGTLTIS NFAVSDFGKL YRSCGNCSTQ
YKRNVVVKNI AVTYPGSSLV GINSNFGDTA TLSGVTITGD KSKKISICVT YKGNKTGAEP
TKLATYKGST GGDGTSCKFT TSNITYK
//
