CAZyme Information: MGYG000001697_01221

Basic Information

• Species: Erysipelatoclostridium saccharogumia
• Lineage: Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Erysipelatoclostridium; Erysipelatoclostridium saccharogumia
• CAZyme ID: MGYG000001697_01221
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1670		184659.61	4.2878

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001697	3141483	Isolate	Germany	Europe

• Gene Location: Start: 28693; End: 33705 Strand: -

Full Sequence      

MKKILKGSLVLALTLSCVPMNTNKLDALAASDIEVTNSNNIVTIGNEYIEREFSTVDNKL
KTTSIENKRAKTTFEPATGSEEFIIKTTKEQKDAPVVPALNRNGWTATADSFHNPSGPSD
GPAQNLLDGDVNSIWHTNYGGGTGDQEYPHNVVINLKGEETFQAFSYTPRQQGEETNGNI
QGYELWVYNGPVGDDLAVDSSEWKQVAKGNFVYEGVNPIYVNLKEATTATQIKFVATSSN
NGAKFAGGAEFNLHAEKAPVEEDNARSFEASDLTLKENGVTVEDTTATINNIEKIGKKVT
FSFEPYNFKGVDYTVNEVVVMYEGDHFMRKYMEISVPDEHAGEAEIDYIDLESLNVNESD
ATWTIPTGKGGVVEMDEFKANLGQPIYIQGMFMGCEFPATDTQIVDDNGYIRYYTGKTFN
KLVDDKQATSNDGMTNYMTWQTVAGAARSTDNSVIQADFYDYIQSIATPSEFRIQYNSWF
DNMMRIDDKNILDSFIEVDRELSNTGVRPLDSYVVDDGWNNYNDTHVVDAVRSGTTLNQT
GFWEFNSKFPQGLTPSSELVNNFGSNFGVWVGPRGGYNFYSSLADILVKNGTGSKAGGSI
DVADRNYIKNFQEMAVNWQKEYKVNYWKWDGFADRAQFNAFPARDGVPGYANNHMTGGYK
NMYHVTDMWEAWIDLFEAVRQSEIDDNINDLWISLTCYVNPSPWYLQWANSVWIQCTHDR
GDAGPINNKMDTMLTYREAVYYDFIKEHEFQFPLANLYNHDPVYGVEGTQININSMTDEQ
FKNYLYMMSTRGTGFWELYYSDSIMTKGKYEVNAEFLAWAEENFHILKNAKMFGGNPANG
VKLGGIGQSTEFEAYGFSAWDGEDGIISMRNPDDEVQTITFTLDRNIGLAESIKDKTLYS
TGIHSYNMPESGNDNYKEFTYGQEVTVTLQPGETRLWSLSTTKDVEAPTYTTLSTDGDKT
LNVKFDEKVIGTDFDVTVNGKVAEIANVSKSVDQVFYEIELATKPTNNATVVVTAKDISD
LNGNKVAKAEKSVIFHKNNTALSVKSDEVTGSKVVGTVAKSLSNDNGFSVVVDVNTTTTN
KELASQGYTVGINAEGKAYFTLGNATATSKVVVNDGTDHQIQAIKENNGILKLYVDGALQ
SSAYDKDNKTLVIEAAKTILGSDGFEGKLGIKVLDRALGYNEFTTDSSEEGLISNENIKP
TATTYDSTEGAVANNANDANTNTYWASAQTANNKTEKQYLTYELSNAYTVNKVQYIPRFD
ATQKLNCTGNILEYVVETSMDGQEWKQVATGATVREGNGVTDIIFESPVEAKYVRLSAND
TYHWKQGSNNTIVAAAEFKVYGKIELDTDALSQRIEELEKVDTTNCTEESIEEFNTLLDE
ARDVLENATDQEEIAQMVEALKNAEGILKPNEPAKEADKTLLKIALDLANAITDEDLANV
VPAVVEEFKEARDEANGIYNDTSATQDKVNAAFDRLATAMHMLDFVKGDKTALKAFIDKV
SGLEASKYTEATWVPFNEALVVATGVYNDENAMQEEITKVYNELVTAFINLRLIPDKTLL
EDLINKANGLSAANYTKASYKVLSDALNDAKVVFDISNATQEEVDSAKDVLAKAIAGLQT
VTTDNTVSTPVNKGDTIVSVKTGDNGLVGMFATMALLSAAGYTAFRRKVD

Enzyme Prediction     

No EC number prediction in MGYG000001697_01221.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM32	1202	1338	3.1e-22	0.9193548387096774
CBM32	113	251	6.6e-17	0.9112903225806451

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00754	F5_F8_type_C	7.39e-13	119	251	10	127	F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
pfam00754	F5_F8_type_C	2.23e-12	1224	1338	25	127	F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
cd14791	GH36	7.58e-08	474	684	4	194	glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
pfam02065	Melibiase	1.83e-05	452	573	17	126	Melibiase. Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan GH-D. Glycoside hydrolase family 36 can be split into 11 families, GH36A to GH36K. This family includes enzymes from GH36A-B and GH36D-K and from GH27.
COG3345	GalA	2.57e-04	459	630	274	441	Alpha-galactosidase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCC62414.1	2.58e-312	74	1199	1	1167
ATD48595.1	5.12e-232	3	1513	5	1521
SQG39183.1	1.40e-231	3	1513	5	1521
SQI04569.1	1.95e-231	3	1513	5	1521
AOY54034.1	5.33e-231	3	1513	5	1521

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2J7M_A	5.68e-15	1198	1342	11	149	Characterizationof a Family 32 CBM [Clostridium perfringens]
2J1A_A	5.83e-15	1198	1342	12	150	Structureof CBM32 from Clostridium perfringens beta-N- acetylhexosaminidase GH84C in complex with galactose [Clostridium perfringens ATCC 13124],2J1E_A High Resolution Crystal Structure of CBM32 from a N-acetyl-beta- hexosaminidase in complex with lacNAc [Clostridium perfringens ATCC 13124]
2V5D_A	1.82e-13	1192	1342	593	737	Structureof a Family 84 Glycoside Hydrolase and a Family 32 Carbohydrate-Binding Module in Tandem from Clostridium perfringens. [Clostridium perfringens]
4LKS_A	1.22e-10	1215	1343	42	167	Structureof CBM32-3 from a family 31 glycoside hydrolase from Clostridium perfringens in complex with galactose [Clostridium perfringens ATCC 13124],4LKS_C Structure of CBM32-3 from a family 31 glycoside hydrolase from Clostridium perfringens in complex with galactose [Clostridium perfringens ATCC 13124],4LQR_A Structure of CBM32-3 from a family 31 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens ATCC 13124],4P5Y_A Structure of CBM32-3 from a family 31 glycoside hydrolase from Clostridium perfringens in complex with N-acetylgalactosamine [Clostridium perfringens ATCC 13124]
1W8N_A	4.01e-07	109	257	466	601	Contributionof the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens. [Micromonospora viridifaciens],1W8O_A Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens [Micromonospora viridifaciens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P0DTR4	2.98e-14	100	303	509	698	A type blood N-acetyl-alpha-D-galactosamine deacetylase OS=Flavonifractor plautii OX=292800 PE=1 SV=1
Q0TR53	3.54e-14	1192	1361	623	787	O-GlcNAcase NagJ OS=Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A) OX=195103 GN=nagJ PE=1 SV=1
Q8XL08	8.00e-14	1192	1361	623	787	O-GlcNAcase NagJ OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagJ PE=1 SV=1
E8MGH9	1.95e-12	1418	1668	1667	1931	Beta-L-arabinobiosidase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=hypBA2 PE=1 SV=1
P26831	8.02e-09	1446	1616	1384	1566	Hyaluronoglucosaminidase OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagH PE=1 SV=2

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
0.000621	0.635390	0.363227	0.000239	0.000281	0.000234

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001697_01221.