ID A0A0N1NNA1_9ACTN Unreviewed; 557 AA.
AC A0A0N1NNA1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=rhamnogalacturonan endolyase {ECO:0000256|ARBA:ARBA00012437};
DE EC=4.2.2.23 {ECO:0000256|ARBA:ARBA00012437};
DE Flags: Precursor;
GN ORFNames=OK074_1614 {ECO:0000313|EMBL:KPI18415.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI18415.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPI18415.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPI18415.1,
RC ECO:0000313|Proteomes:UP000037991};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) 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:KPI18415.1}.
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DR EMBL; LJCV01000066; KPI18415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1NNA1; -.
DR PATRIC; fig|1592327.3.peg.2055; -.
DR OrthoDB; 7169863at2; -.
DR Proteomes; UP000037991; 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; 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; IPR016590; Rhamnogalacturonase_B.
DR InterPro; IPR015364; RhgB_N.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR36574; RHAMNOGALACTURONATE LYASE-RELATED; 1.
DR PANTHER; PTHR36574:SF1; RHAMNOGALACTURONATE LYASE-RELATED; 1.
DR Pfam; PF14683; CBM-like; 1.
DR Pfam; PF14686; fn3_3; 1.
DR Pfam; PF09284; RhgB_N; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000037991};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..557
FT /note="rhamnogalacturonan endolyase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039340109"
FT DOMAIN 38..287
FT /note="Rhamnogalacturonase B N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09284"
FT DOMAIN 293..369
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14686"
FT DOMAIN 386..555
FT /note="Rhamnogalacturonan lyase"
FT /evidence="ECO:0000259|Pfam:PF14683"
SQ SEQUENCE 557 AA; 58466 MW; 0CD3794529D301FA CRC64;
MSGPRPLGRR AFVIGTAATA GSAALAGPLA VNSQAASFGY TDDGSNYVID TGALLVFKVS
KTNGDLTSLV YRGTEYQGYG GMNSHVESGL GASTVTIAQS GSTILVSVTH GTLKHYYAAR
SGENNVYLWT NKADTSVSAT RYIVRVKAGM FLNDEPDSYT YTTSTIEASD VFAKSDGQTR
SKHYSKLRVI DYDYIGWTTG SVGLYVVRSN HEKASGGPFY RSLLRHQSAD GGGLYEILYY
GENQTEAQRF GLQGPYVIAF TDGGAPSSSL YHGNLTTSWA DSLGISGYVA AGGRGRVAGV
AITGRDTTSA YTVGIANSAA QYWGSARSSD GYFSIPGALP GTYTLTVFKG ELAVYTTSVT
VTAGGTTTLN TIAIPSSNDP SNASAIWRIG DWDGTPSGFK NAALMTYAHP SDPRAASWTG
NVVIGSGSET SAFPCYLWKD VNSGIIVYFK LTAAQAAAAH TLRIGVTTAY ANGRPQVVVN
DTWTSAVPSP PTQPSTRSLT VGSYRGNNYT FSYSVPASAW LTDTSAYNTL KIYVASGSGS
TSYLSAGTSV DALDLLA
//
