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CAZyme Information: MGYG000003625_01426

You are here: Home > Sequence: MGYG000003625_01426

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species UBA2913 sp900770895
Lineage Bacteria; Firmicutes_C; Negativicutes; Selenomonadales; Selenomonadaceae; UBA2913; UBA2913 sp900770895
CAZyme ID MGYG000003625_01426
CAZy Family PL4
CAZyme Description Rhamnogalacturonate lyase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
585 MGYG000003625_192|CGC1 65579.57 5.3626
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003625 2467170 MAG Fiji Oceania
Gene Location Start: 17677;  End: 19434  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003625_01426.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL4 33 579 4.4e-186 0.9909255898366606

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd10320 RGL4_N 2.06e-58 33 294 4 262
N-terminal catalytic domain of rhamnogalacturonan lyase, a family 4 polysaccharide lyase. The rhamnogalacturonan lyase of the polysaccharide lyase family 4 (RGL4) is involved in the degradation of RG (rhamnogalacturonan) type-I, an important pectic plant cell wall polysaccharide, by cleaving the alpha-1,4 glycoside bond between L-rhamnose and D-galacturonic acids in the backbone of RG type-I through a beta-elimination reaction. RGL4 consists of three domains, an N-terminal catalytic domain, a middle domain with a FNIII type fold and a C-terminal domain with a jelly roll fold; the middle and C-terminal domains are both putative carbohydrate binding modules. There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain (RG chain) through the beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11.
pfam14683 CBM-like 3.55e-33 429 581 1 157
Polysaccharide lyase family 4, domain III. CBM-like is domain III of rhamnogalacturonan lyase (RG-lyase). The full-length protein specifically recognizes and cleaves alpha-1,4 glycosidic bonds between l-rhamnose and d-galacturonic acids in the backbone of rhamnogalacturonan-I, a major component of the plant cell wall polysaccharide, pectin. This domain possesses a jelly roll beta-sandwich fold structurally homologous to carbohydrate binding modules (CBMs), and it carries two sulfate ions and a hexa-coordinated calcium ion.
cd10317 RGL4_C 1.94e-32 431 579 1 158
C-terminal domain of rhamnogalacturonan lyase, a family 4 polysaccharide lyase. The rhamnogalacturonan lyase of the polysaccharide lyase family 4 (RGL4) is involved in the degradation of RG (rhamnogalacturonan) type-I, an important pectic plant cell wall polysaccharide, by cleaving the alpha-1,4 glycoside bond between L-rhamnose and D-galacturonic acids in the backbone of RG type-I through a beta-elimination reaction. RGL4 consists of three domains, an N-terminal catalytic domain, a middle domain with a FNIII type fold and a C-terminal domain with a jelly roll fold. Both the middle and the C-terminal domain are putative carbohydrate binding modules. There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain (RG chain) through the beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11.
cd10316 RGL4_M 1.45e-15 325 419 1 91
Middle domain of rhamnogalacturonan lyase, a family 4 polysaccharide lyase. The rhamnogalacturonan lyase of the polysaccharide lyase family 4 (RGL4) is involved in the degradation of RG (rhamnogalacturonan) type-I, an important pectic plant cell wall polysaccharide, by cleaving the alpha-1,4 glycoside bond between L-rhamnose and D-galacturonic acids in the backbone of RG type-I through a beta-elimination reaction. RGL4 consists of three domains, an N-terminal catalytic domain, a middle domain with a FNIII type fold and a C-terminal domain with a jelly roll fold. Both the middle domain represented by this model and the C-terminal domain are putative carbohydrate binding modules. There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain (RG chain) through the beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11.
pfam13620 CarboxypepD_reg 1.52e-07 328 417 1 77
Carboxypeptidase regulatory-like domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
APC39134.1 7.45e-172 34 583 9 563
ASG79905.1 3.84e-135 40 583 11 560
BBD17486.1 3.66e-130 34 581 5 548
BAL62737.1 3.66e-130 34 581 5 548
BBD14740.1 3.66e-130 34 581 5 548

PDB Hits      help

has no PDB hit.

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8RJP2 3.05e-124 33 582 32 574
Rhamnogalacturonate lyase OS=Dickeya dadantii (strain 3937) OX=198628 GN=rhiE PE=1 SV=1
A5ABH4 1.06e-31 129 566 129 632
Probable rhamnogalacturonate lyase B OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=rglB PE=3 SV=1
Q5AZ85 2.10e-31 107 565 104 628
Rhamnogalacturonate lyase B OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=rglB PE=2 SV=2
A1D144 7.01e-30 64 475 60 502
Probable rhamnogalacturonate lyase B OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=rglB PE=3 SV=1
B0XPA2 9.67e-29 64 566 60 627
Probable rhamnogalacturonate lyase B OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=rglB PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000245 0.999062 0.000159 0.000184 0.000163 0.000143

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003625_01426.