ID Q2SHE7_HAHCH Unreviewed; 523 AA.
AC Q2SHE7;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=pectin lyase {ECO:0000256|ARBA:ARBA00039082};
DE EC=4.2.2.10 {ECO:0000256|ARBA:ARBA00039082};
GN OrderedLocusNames=HCH_03164 {ECO:0000313|EMBL:ABC29927.1};
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521 {ECO:0000313|EMBL:ABC29927.1, ECO:0000313|Proteomes:UP000000238};
RN [1] {ECO:0000313|EMBL:ABC29927.1, ECO:0000313|Proteomes:UP000000238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396 {ECO:0000313|EMBL:ABC29927.1,
RC ECO:0000313|Proteomes:UP000000238};
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(2005).
CC -!- FUNCTION: Pectinolytic enzymes consist of four classes of enzymes:
CC pectin lyase, polygalacturonase, pectin methylesterase and
CC rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the
CC most important in depolymerization of pectin, since it cleaves internal
CC glycosidic bonds of highly methylated pectins.
CC {ECO:0000256|ARBA:ARBA00037631}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Eliminative cleavage of (1->4)-alpha-D-galacturonan methyl
CC ester to give oligosaccharides with 4-deoxy-6-O-methyl-alpha-D-
CC galact-4-enuronosyl groups at their non-reducing ends.; EC=4.2.2.10;
CC Evidence={ECO:0000256|ARBA:ARBA00036818};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU361173}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC {ECO:0000256|RuleBase:RU361173}.
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DR EMBL; CP000155; ABC29927.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2SHE7; -.
DR STRING; 349521.HCH_03164; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; PL1; Polysaccharide Lyase Family 1.
DR KEGG; hch:HCH_03164; -.
DR eggNOG; COG3866; Bacteria.
DR HOGENOM; CLU_039498_0_0_6; -.
DR Proteomes; UP000000238; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030570; F:pectate lyase activity; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR002022; Pec_lyase.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR045032; PEL.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR31683; PECTATE LYASE 18-RELATED; 1.
DR PANTHER; PTHR31683:SF67; PECTIN LYASE F-RELATED; 1.
DR Pfam; PF00544; Pectate_lyase_4; 1.
DR Pfam; PF14200; RicinB_lectin_2; 2.
DR SMART; SM00656; Amb_all; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361173};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361173};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361173};
KW Reference proteome {ECO:0000313|Proteomes:UP000000238};
KW Secreted {ECO:0000256|RuleBase:RU361173}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..523
FT /note="pectin lyase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004215469"
FT DOMAIN 40..175
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT DOMAIN 245..464
FT /note="Pectate lyase"
FT /evidence="ECO:0000259|SMART:SM00656"
SQ SEQUENCE 523 AA; 56789 MW; 1B8E6851051F9FFD CRC64;
MNMKTHRIGF CVVSLSLLAG TLLSPSYAEA ANCEATPISG KTYSIVNRET GLVLDISGYS
KADGAAVVQW RAKGSANQKF RVTDVGGGAL KIEAIHSNLA LDVLYLAQHD NAELIQWPYW
GGLNQQWSLV KSSTGGYSIR ARHTEKALTA QSRDMGARIV QSADIGSGLQ RWYFNPVDGE
CSQASGFAGQ KGADGLAATT GGAGGATVVA ANCQTLTTAL TSEGAKTVIV PDNTAIDCRT
PVRKVSACAM TCPSYQDQNK TFYRVPVGSQ TCTELGGATN DTVSVNRDES RIHIKSDKTL
MGQGANSRII GATLIINGVK NIIVKNLTIE GVNPHLVEAG DGITIENASH IWVDHIRTRM
ISDGHIDIRN SRNLTLSWNH FDGYNPYVCG NQHHYTMLAQ DSQVTIDHNF WDRASGRNPK
LYGWDTRAHI YNNYWNNITY FSISTSNGAQ GLIQNNHFEN ARSPHWNESG YMSASGNVYT
SSSATDPKRD EGDSVFYDID MYPYKLDSAA NLPSVLKSQT GPR
//
