ID A0A178IDG6_9BACT Unreviewed; 629 AA.
AC A0A178IDG6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
GN ORFNames=AW736_19710 {ECO:0000313|EMBL:OAM88064.1};
OS Opitutaceae bacterium TSB47.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX NCBI_TaxID=1184151 {ECO:0000313|EMBL:OAM88064.1, ECO:0000313|Proteomes:UP000078486};
RN [1] {ECO:0000313|EMBL:OAM88064.1, ECO:0000313|Proteomes:UP000078486}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSB47 {ECO:0000313|EMBL:OAM88064.1,
RC ECO:0000313|Proteomes:UP000078486};
RA Wang Y., Shi Y., Qiu Z., Liu S., Yang H.;
RT "High potential of lignocellulose degradation of a new Verrucomicrobia
RT species.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-
CC (1->4)-alpha-D-galactopyranosyluronic acid bonds of
CC rhamnogalacturonan I domains in ramified hairy regions of pectin
CC leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-
CC unsaturated D-galactopyranosyluronic acid at the non-reducing end.;
CC EC=4.2.2.23; Evidence={ECO:0000256|ARBA:ARBA00001324};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 4 family.
CC {ECO:0000256|ARBA:ARBA00010418}.
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:OAM88064.1}.
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DR EMBL; LRRQ01000148; OAM88064.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178IDG6; -.
DR STRING; 1184151.AW736_19710; -.
DR OrthoDB; 101122at2; -.
DR Proteomes; UP000078486; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0102210; F:rhamnogalacturonan endolyase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR CDD; cd10317; RGL4_C; 1.
DR CDD; cd10316; RGL4_M; 1.
DR CDD; cd10320; RGL4_N; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR029413; RG-lyase_II.
DR InterPro; IPR029411; RG-lyase_III.
DR InterPro; IPR010325; Rhamnogal_lyase.
DR PANTHER; PTHR32018:SF1; RHAMNOGALACTURONAN ENDOLYASE; 1.
DR PANTHER; PTHR32018; RHAMNOGALACTURONATE LYASE FAMILY PROTEIN; 1.
DR Pfam; PF14683; CBM-like; 1.
DR Pfam; PF14686; fn3_3; 1.
DR Pfam; PF06045; Rhamnogal_lyase; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000078486};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..629
FT /note="rhamnogalacturonan endolyase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008088667"
FT DOMAIN 374..443
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14686"
FT DOMAIN 459..619
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14683"
SQ SEQUENCE 629 AA; 68281 MW; E4B854D42479AA3A CRC64;
MKIIRVVLVA ACMLASSICF ANVPGGGSGN GPDVSLKDEG DSIVLDNGIV AIRINKTDAS
VRSFIYQGMN LFEGGHGGGR FYWSWNTPAY GGPHGTAMVT ADPASNHGDY AEVKVHSPWS
GKSADAAMDV DIYYSLKRGT QGYYATAMLN HPATYPRADV GEWRSNAYIS PIFDWLSVDA
LRQRKMPTLE DMVASVPVEG APKEVTLLTS GIYAGQFECK YSYSADLGDL NVWGWSSTSK
RVGIWMTIPS HEYYNGGPMK RELTGHMNHA LLNMLNGSHY SQGTQLIMAD GNVFKKTYGP
FFVYANSYQG AASDSSSKVV ESLWHDAQAQ AVAERSAWPY RWFKNADYVQ ESGRGTVSGT
LKVSDGGNPA AIAAGAWIGL APDDNGTDFQ LQGRTYQFWV KTSADGRFNI PHVLPGVYHL
WAFGAGNIGT FKQANIEVSA GKALDVGTVL WTPPRVADTL WEIGIPDRDS QEFHNGAFNY
TQWATFAKSR SESESGLTYT VGKSDWRKDW NYAQFGPTPW TIKFSLADKP AKDAPASLYI
ALASSESTLM VTVNGTQIGT YKTPHPAHAP IRLGSHGPFA ETRIAIPPGL LKRGTNTIAI
SQVMGKGKTG TTQYDYLRLE AAGTRLAAP
//
