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CAZyme Information: MGYG000004003_02798

You are here: Home > Sequence: MGYG000004003_02798

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
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides;
CAZyme ID MGYG000004003_02798
CAZy Family GH16
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
887 MGYG000004003_51|CGC1 101300.86 5.0051
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004003 5653807 MAG United Kingdom Europe
Gene Location Start: 22165;  End: 24828  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004003_02798.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH16 544 828 3.4e-19 0.9841269841269841

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam07980 SusD_RagB 2.01e-30 303 543 18 272
SusD family. This domain is found in bacterial cell surface proteins such SusD and SusD-like proteins, as as well RagB, outer membrane surface receptor antigen. Bacteroidetes, one of the two dominant bacterial phyla in the human gut, are Gram-negative saccharolytic microorganisms that utilize a diverse array of glycans. Hence, they express starch-utilization system (Sus) for glycan uptake. SusD has 551 amino acids, and is almost entirely alpha-helical, with 22 alpha-helices, eight of which form 4 tetra-trico peptide repeats (TPRs: helix-turn-helix motifs involved in protein-protein interactions). The four TPRs pack together to create a right-handed super-helix. This is predicted to mediate the formation of SusD and SusC porin complex at the cell surface. The interaction between SusC and TPR1/TPR2 region of SusD is predicted to be of functional importance since it allows SusD to be in position for oligosaccharide capture from other Sus lipoproteins and delivery of these glycans to the SusC porin. The non-TPR containing portion of SusD is where starch binding occurs. The binding site is a shallow surface cavity located on top of TPR1. SusD homologs such as SusD-like proteins have a critical role in carbohydrate acquisition. Both SusD and its homologs, contain about 15-20 residues at the N-terminus that might be a flexible linker region, anchoring the protein to the membrane and the glycan-binding domain. Other homologs to SusD have been examined in Porphyromonas gingivalis such as RagB, an immunodominant outer-membrane surface receptor antigen. Structural characterization of RagB shows substantial similarity with Bacteroides thetaiotaomicron SusD (i.e alpha-helices and TPR regions). Based on this structural similarity, functional studies suggest that, RagB binding of glycans occurs at pockets on the molecular surface that are distinct from those of SusD.
cd08977 SusD 1.76e-21 48 499 6 358
starch binding outer membrane protein SusD. SusD-like proteins from Bacteroidetes, members of the human distal gut microbiota, are part of the starch utilization system (Sus). Sus is one of the large clusters of glycosyl hydrolases, called polysaccharide utilization loci (PULs), which play an important role in polysaccharide recognition and uptake, and it is needed for growth on amylose, amylopectin, pullulan, and maltooligosaccharides. SusD, together with SusC, a predicted beta-barrel porin, forms the minimum outer-membrane starch-binding complex. The adult human distal gut microbiota is essential for digestion of a large variety of dietary polysaccharides, for which humans lack the necessary glycosyl hydrolases.
cd08023 GH16_laminarinase_like 4.98e-15 546 829 3 235
Laminarinase, member of the glycosyl hydrolase family 16. Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans.
pfam14322 SusD-like_3 1.69e-08 26 235 1 185
Starch-binding associating with outer membrane. SusD is a secreted polysaccharide-binding protein with an N-terminal lipid moiety that allows it to associate with the outer membrane. SusD probably mediates xyloglucan-binding prior to xyloglucan transport in the periplasm for degradation. This domain is found N-terminal to pfam07980.
NF033071 SusD 5.09e-08 153 472 151 487
starch-binding outer membrane lipoprotein SusD. SusD (Starch Uptake System D) is an outer membrane lipoprotein that binds starch and participates in a TonB-dependent nutrient uptake complex. Related proteins from similar TonB-dependent complexes that import other, usually multimeric nutrient substrates include RagB and NanU.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QRQ57561.1 0.0 1 887 1 887
ALJ45968.1 0.0 1 887 1 887
QDH56574.1 0.0 1 887 1 887
SCV10319.1 0.0 410 887 1 478
QRQ57560.1 9.28e-77 530 866 23 360

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3QNK_A 7.50e-36 97 505 67 466
Crystalstructure of a SusD-like protein (BF3747) from Bacteroides fragilis NCTC 9343 at 2.70 A resolution [Bacteroides fragilis NCTC 9343],3QNK_B Crystal structure of a SusD-like protein (BF3747) from Bacteroides fragilis NCTC 9343 at 2.70 A resolution [Bacteroides fragilis NCTC 9343],3QNK_C Crystal structure of a SusD-like protein (BF3747) from Bacteroides fragilis NCTC 9343 at 2.70 A resolution [Bacteroides fragilis NCTC 9343],3QNK_D Crystal structure of a SusD-like protein (BF3747) from Bacteroides fragilis NCTC 9343 at 2.70 A resolution [Bacteroides fragilis NCTC 9343]
3I4G_A 3.50e-29 31 512 18 474
CRYSTALSTRUCTURE OF A SUSD-LIKE CARBOHYDRATE BINDING PROTEIN (BF0978) FROM BACTEROIDES FRAGILIS NCTC 9343 AT 1.35 A RESOLUTION [Bacteroides fragilis NCTC 9343]
5CJZ_A 5.49e-28 90 554 78 617
BT4246with galactose [Bacteroides thetaiotaomicron VPI-5482],5CK0_A Bt4246 [Bacteroides thetaiotaomicron VPI-5482]
5CK1_A 7.90e-28 90 554 93 632
selenomethionineBT4246 [Bacteroides thetaiotaomicron VPI-5482]
7BLL_A 1.32e-26 49 515 41 592
ChainA, SusD homolog [Bacteroides thetaiotaomicron VPI-5482]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
T2KNB8 5.90e-15 23 501 19 477
SusD-like protein P25 OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22140 PE=2 SV=1
T2KN63 1.12e-12 104 523 102 481
SusD-like protein P2 OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_21910 PE=2 SV=1
T2KPM5 3.15e-11 1 507 1 472
SusD-like protein P38 OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22270 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000000 1.000063 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004003_02798.