CAZyme Information: MGYG000004003_02798

Basic Information

• 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      

MKYPVGLSIILNALAAISILSGCSDYLDREYDSFIDNEMTFTSYERTSKFLVNAYRYLPD
GFNRIGSEAMLDAATDDAEHANASCNIQHFNTGAWNSRSNPDDLWNKYYAGIRIANEFIE
NVGRVNLDKYRLDPDNQNEYQNRLNDLKTWKYEARFLRAFFHFELVKRFGPVPVITSTLS
VNADYSETPRPLMDDCISFISSECDKVAEVLDLTPGRGIDSDLGRATKGAALALKSRVLL
YAASPLYLDWQNLSESYLPSDMEKWKAAAQAAKDVIDLGVYSLYGNYATLFKNNFQNSEF
ILMRRYGNSSDFEKYNFPVSYGGIGGINPSLNLVDSYEMKDGSYFCWENEENALRPQFYR
DDRLNATILLNDSAWKSTVVENWDGGKDGLGVTNATKTGFYLKKYLNEDVNIQTGGGSQG
HIWPLFRLAEIYLNYAEALNECDPENSDIAEYVNRVRSRAGQPNLPSGLTQDEMRERIRR
ERRVELAFEEHRSWDVRRWKIAQETLGGDLLGLEITRKSQARRAVTRNSIIPANEIPEGW
HYYDGDEFNDLVINNSYWGQYGSDTPVGNSQYGQPTGNIQTYRRKQITIEKGSGGLSFAR
IAATKDDNPPAPALSTASTREGWWSGALSSRDTDKYGYQGKYYPLHSRIEIRAKIPYIYG
IWMGPWCRHYAGASVAELDIEEFFVKEFENTVSPRRLSQALHLHDNKTGNLGVNVNGYGR
HTVLDFDPGSDFHTYGVQVDPDPVSPDKHAIISYLLDGKVTNTFKTIDYDDRYNTFITKA
IAEGREKRTWDIAITGQIGGKNENGIGYPEDRNANLRNVSMDVDWVRVFTRDEIEPEIPE
KPEYPVEKFYYSRAVVEKRVFDSKMYWYPIPESEILQLKNWKQNPGW

Enzyme Prediction     

No EC number prediction in MGYG000004003_02798.

CAZyme Signature Domains

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

CDD Domains     

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     

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     

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     

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

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     

There is no transmembrane helices in MGYG000004003_02798.