CAZyme Information: MGYG000000265_01678

Basic Information

• Species: Bacteroides nordii
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides nordii
• CAZyme ID: MGYG000000265_01678
• CAZy Family: GH97
• CAZyme Description: Retaining alpha-galactosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
758	MGYG000000265_5|CGC1	86450.47	5.1456

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000265	5489209	Isolate	China	Asia

• Gene Location: Start: 96093; End: 98369 Strand: +

Full Sequence      

MNRKSILSLLFLFFCTFGVQAEEYETTSPNGTLKIKLRVDNGTTYEVWHGDKQLIAPSSI
GLNLSNGTIVGGGTVKSTTTNHVDQTIDVVAGKNKTLREAYNELLISFNENYDLLVRAYD
EGIAYRFITRLDGEIIINSEDAVFNFTSTPTIYFPECDTNYSGEKDQQGKVHQIHQGYRN
FERLYKTYNAPTDITNNRFSVSPVLFSYPDTPYKIVVTESDTYDYPGLYMEQNGVNSMRG
KWAQYPKEVMDSDPSNSSYWYSNHLVISRENYIAKTEGSRTFPWRVIIVSDDDKSLLNNE
LVYMLAEPCRLTDTSWIQPGKSAWEWWHKAVLEGVDFPSGNKNLSFQLYKYYVDWASQHC
IEYMTLDAGWSEDYIRTLCLYAKQKNVKILVWTWASCVRENPQDWIKKMKDYGVSGAKID
FFERSDQIAMRWGREFAQRLADNQMVALFHGCPVPTGINRTYPNILNFEAVRGAECNFWE
STLTPEYHTQFPFIRSLAGPEDYTPGSMRNVTQEEFKPIDKDNTPPMSMGTRAHELSMYV
IYDQWVGYLCDSPTEYNKYPDILSFLSTVPTIWDKTVPLDAKLGDYILMAKQKGKDWYVG
GMTDWTPRTVEIDFSFLEAGASYQADIFKDAPASGEQPKEYVCEKMEITKDTKLSINMAK
GGGFAIRLLHSSGSGIAKVNQENPLTVYVEKESDTLHVKTKKIIEAVKINNISGQVLFAK
NFKDGSYSEQIDLSGFNRGVYVVSVKTEAALASTTFIY

Enzyme Prediction     

No EC number prediction in MGYG000000265_01678.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH97	12	668	1.4e-181	0.993660855784469

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam10566	Glyco_hydro_97	3.34e-100	313	570	1	278	Glycoside hydrolase 97. This domain is the catalytic region of the bacterial glycosyl-hydrolase family 97. This central part of the GH97 family protein sequences represents a typical and complete (beta/alpha)8-barrel or catalytic TIM-barrel type domain. The N- and C-terminal parts of the sequences, mainly consisting of beta-strands, form two additional non-catalytic domains. In all known glycosidases with the (beta-alpha)8-barrel fold, the amino acid residues at the active site are located on the C-termini of the beta-strands.
pfam14508	GH97_N	7.78e-59	28	308	1	235	Glycosyl-hydrolase 97 N-terminal. This N-terminal domain of glycosyl-hydrolase-97 contributes part of the active site pocket. It is also important for contact with the catalytic and C-terminal domains of the whole.
pfam14509	GH97_C	6.63e-45	573	668	1	96	Glycosyl-hydrolase 97 C-terminal, oligomerization. Glycosyl-hydrolase-97 is made up of three tightly linked and highly conserved globular domains. The C-terminal domain is found to be necessary for oligomerization of the whole molecule in order to create the active-site pocket and the Ca++-binding site.
pfam18962	Por_Secre_tail	3.00e-08	693	757	7	71	Secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber have on average twenty or more copies of this C-terminal domain, associated with sorting to the outer membrane and covalent modification. This domain targets proteins to type IX secretion systems and is secreted then cleaved off by a C-terminal signal peptidease. Based on similarity to other families it is likely that this domain adopts an immunoglobulin like fold.
TIGR04183	Por_Secre_tail	2.86e-05	691	757	7	70	Por secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT73254.1	0.0	1	668	1	670
QUT41086.1	0.0	1	668	1	670
AAO78269.1	0.0	1	668	1	670
QMW85572.1	0.0	1	668	1	670
BCA52479.1	0.0	1	668	1	670

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3A24_A	9.63e-142	28	668	6	640	Crystalstructure of BT1871 retaining glycosidase [Bacteroides thetaiotaomicron],3A24_B Crystal structure of BT1871 retaining glycosidase [Bacteroides thetaiotaomicron]
5E1Q_A	1.62e-140	28	668	20	654	Mutant(D415G) GH97 alpha-galactosidase in complex with Gal-Lac [Bacteroides thetaiotaomicron VPI-5482],5E1Q_B Mutant (D415G) GH97 alpha-galactosidase in complex with Gal-Lac [Bacteroides thetaiotaomicron VPI-5482]
5HQ4_A	3.33e-52	28	667	5	657	AGlycoside Hydrolase Family 97 enzyme from Pseudoalteromonas sp. strain K8 [Pseudoalteromonas sp. K8],5HQA_A A Glycoside Hydrolase Family 97 enzyme in complex with Acarbose from Pseudoalteromonas sp. strain K8 [Pseudoalteromonas sp. K8]
5HQC_A	3.33e-52	28	667	5	657	AGlycoside Hydrolase Family 97 enzyme R171K variant from Pseudoalteromonas sp. strain K8 [Pseudoalteromonas sp. K8]
5HQB_A	8.44e-52	28	667	5	657	AGlycoside Hydrolase Family 97 enzyme (E480Q) in complex with Panose from Pseudoalteromonas sp. strain K8 [Pseudoalteromonas sp. K8]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8A6L0	1.32e-144	4	668	2	661	Retaining alpha-galactosidase OS=Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) OX=226186 GN=BT_1871 PE=1 SV=1
G8JZS4	7.89e-53	1	678	1	733	Glucan 1,4-alpha-glucosidase SusB OS=Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50) OX=226186 GN=susB PE=1 SV=1
D7CFN7	1.65e-47	3	670	6	622	Probable retaining alpha-galactosidase OS=Streptomyces bingchenggensis (strain BCW-1) OX=749414 GN=SBI_01652 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000244	0.999088	0.000182	0.000171	0.000160	0.000140

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000265_01678.