CAZyme Information: MGYG000001748_00828

Basic Information

• Species: CAG-56 sp900762665
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-56; CAG-56 sp900762665
• CAZyme ID: MGYG000001748_00828
• CAZy Family: GH146
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
3273	MGYG000001748_7|CGC2	354070.11	4.6338

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001748	4218051	MAG	Sweden	Europe

• Gene Location: Start: 61117; End: 70938 Strand: +

Full Sequence      

MNRAISLLMVITMLSAILLSALPALPVSAATGLDLTKYDPYGAEDGNIALSAKVEAVYSN
GSSVARNANNGTLGNGGTNTVWNTWGTQYGNPGNPVWIQYTWDQPYVIEATRVMWWIYTD
AGVRWARDCKLQYQKDGEWIDCGSIGTDGNSANFSGGAEVNKPWPAPGRWGTNTVWNPLE
LEETIVTTGLRLSITAERDSGSAPGVGISEWEVFGYVDPAIADLAEIDENFLSELYDDAA
LPTEGTYGSTITWSDSTNTALAVDGTVTRPEIGQEDAVGQITATAVKDDFTATKVFDFTV
KAKMSDKAMVDEDLAAIDLGSTEGRTTNFDLPAEGRFGSVITWSSDNTKYLWNDGTVVRP
PTGQSDVSAILTATATIGTTVETRQWEVRIPAYPPEGRAIVSYDPINVECPAGNAPKLPN
QIKVYYSNGDSELRRIKWEGYSVADQTTQAGYPVGHEYTLNGNIQGDNATVNGYQVAANI
TVVAAEKNNEVPSNEPVAETLPLSKVTLNNDPDGEQNRLTLNTESHIQYILGVDVTRMLY
NYRDTFGLSTEGYATPGGWDSPTTKLKGHGYGHYLSGLALAYASDAKPDEREQLLSRMKR
MTDEMREMQEMTFVKITDEDGVERFREARDRYSNDDEVRAMTNVRLRDDKTAPRDPKLFG
YGYINAIQPEHLILIENYAPYNGNMSDYGVWAPYYALHKQLAGLVEIYNVLNGGNQEEQA
IAEKALLIAKDMGMWVWNRLNYCTHEGKRPNNNTPGYRDTMWGLYIAGEFGGMNETLARL
SDIMKKKGDSDDSAKLLEASTFFDNNGASSDTGNVPFFGSLANNIDSIRTLHCNQHIPQI
VGTLWSFKGSNDPKYYNIAENFWDYVYGRYSFTIGGVGGNDSNEEKFAGTYNQIGVVNTN
DGGKICETCAAYNLLKLTKDLNGYNPDDAKYMDYYERLLYNQIVGSIVPGSKSNQTSYGY
SIYPNTQRSRSTGNATNPGSTCCSGTGTENHVKYQEAAYFTSADNQTFYVGLYIPTTARW
DAQDVSITQSCVFPSEESTFTVAPGAATGKFEMKFRVPYWATKDFDIKLNGKSIADSYEP
SSYVSTGVREWNDKDTVVVTMPYGFNVDYLPGKCDGEWYGSLMNGPLVMAATDVKELSRV
ELDSYMSIGEGTNVLMNERATMTGGTNNEKPTRNVHNMSVKVAPGTSGGEAATKTFVPHY
FAGVPAYTTYFYIPAPNENTGVDKTPLFEKITEATDRIDTGLYSQESVDALKAVLPNAVA
AYQSNETTEKQLNDAIAEVQAGIEKLAALPVEITKLQEKVDEADSVAEGDYTPESYELLS
SKIAEAVAYKEAGNYTDAETAEHIFAIESAMKALVALNKAELIAALEKAAELTNPENTGE
KLWAEHEYTTYTRKSWNAFKAVEESSQKILQNDPKVPAQSEIDGAASELNKAMDALLPYN
LCDEREPLEKAIEKAKTYKNDPPQYDEKAFEALQNAITEAEERLGYASLTFPERDGFIND
LEKAIKDLTNVPSEGVELIRNGKFTAGVSPWVGHWGGANGLSVKDDETVGKYLEVDKKGN
NWNSFYMVKQEVTGDFKVGDVLKYSYKVRSGAANNNQNTRFNIMIANVDGNFVEDNDALH
KKFAGPRVQGDWVTVTGTCEIWADTQKIAFGINENGYSANANNVHLADVSVLYVEDTTSI
RVTGIELNKDALTLSPGAREELIATVKPDDATRKGVLWSSSDPSVAKVDSKGLITAVGVG
TATITATADSDKTIKAECAVTVNEIPVTEVTLNESALSLEPGVKSTLKAAVKPANATNKS
VEWSTSDAKVATVENGVVTAVAVGEAKITAASVSDPTKKAECTVTVTNEKVAATEVTLNS
TRLSMKAGTKKTLVETVKPANATNKNVEWSTSNPSVAAVKDGVVTAVTAGTVMITAKLAT
DPSKRADCLVTVTGSILEQATAANPYLPLWEHLPDGEPNVFEDPDNPGKYRAYIIGSHDL
RRNEYCGPDVRAWSAPVEDLTQWRDEGPIFTHYVNEQWDLIYAPDIVEVRRRDENGDRTI
KEYYLYPHSRGGNRLSMVCKGDSPVGPFTPINLNEAGTATLPGSLVGFDPAVLVDYIDDP
EDPDYEIGFRAYAYWGWQEAEACELDQTNMWAVRPGTERIHDFIPCSTSYGNIRKPDIEY
PYVFPGEDLKSFNYFEAFEIRKVGNKYVLTFSGYSGPDYGMGSTNSALRYAYGDTPLGPW
KSGGVLVDSRGPVLNEAGTGLVGRTWGHNTHGGLQQINDQWYVFYHRPPRGNGNARQAVV
APVKIDWDEKSVADGGKVSIKAYDPYSEDNTWTAKDSQGREYTGAEITSEGFHLYGLDPY
KYYSAGIASYVDGGTLQDSYEIWDSHMPIENVRNNAKIGYKYFGFEGIEEDQKGIKAFEG
TKPGNNTKFNVFLTPKTAESFKVNVWLDGPWDNETWKGTKIGEIEVPAGSAQETQRFQLD
VSDAVDNLDGKHAVFLVAEGGDGNLFDLIGLGFTSDTKEIERPIMPTLSISINGSEMTLP
SLPMASTGKNGIMTYDLYNVNPPSGLTSVPDIEAHASDDNVKITISKPSSLTGIAYVRFE
LNGKTKTYRIPFAKQEYTIFEEMNLGIASVEAASSVIGDMLILDDADSMNDEQKAAKAKE
MIDDMLQEALLENDALRGVAADVTNADGSFVLKLTCGDTEMTNSAFAITSPVTLVPVTKV
TVDKTTLTLVAGNKGTLKAAVQPNDATVQEVLWSSSDESVATVNNGVVTAVAPGKATITV
TSFSDNTKKAECVVTVNDLSPEEQAKKAAEEAKKAAEEAKTQAENAKASAESAKSDALKA
ENDAKSAAGSAETATEEAKKASDAAVTATDEAKKAADEAVKAKAEADKAKADADKAAAEA
GKSETARLAAEAAQKKAEDAQSKAAEAQGKAEAAQTKAETAQSKAAEAQSKAEIAQSNAE
KAKADAETARTKAEEAKDKAVAAQSASEKSAAAAAAAQKAAESANIDAQAAKKAAEAARD
QAISEKDDAVAAAKAAADAKAQTQVIKEQVETIKAQVETIKAEAVAAKTAAESAKADAIA
AKKEAEAAKADAISASADALAAKAAAEAAAKAAEESAAAAKKAEEEAKKAAAEAAEKKKD
AEEARIAAEKAQAAAEAALKAAQAAQAAAEARQKELDLAKQAVADAQKSAKKDSDALALV
RRTAKIKSVKSPSKGKVKVLLNKDKAAVGYQIQYSQKKTFKGGLKTKTVKTTSYTIKSLK
KKTYYVRARAYTTDSKGKRVYSKWSKVRKVRVK

Enzyme Prediction     

No EC number prediction in MGYG000001748_00828.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH146	521	1130	1.7e-124	0.9781312127236581
GH43	1944	2285	5.8e-100	0.9965986394557823

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam07944	Glyco_hydro_127	5.38e-76	506	1102	2	474	Beta-L-arabinofuranosidase, GH127. One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context.
cd18620	GH43_XylA-like	1.27e-68	1954	2288	1	269	Glycosyl hydrolase family 43-like protein such as Clostridium stercorarium alpha-L-arabinofuranosidase XylA. This glycosyl hydrolase family 43 (GH43) subgroup belongs to the GH43_AXH-like subgroup which includes enzymes that have been characterized with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), alpha-1,2-L-arabinofuranosidase 43A (arabinan-specific; EC 3.2.1.-), endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. The GH43_XylA-like subgroup includes Clostridium stercorarium alpha-L-arabinofuranosidase XylA, and enzymes that have been annotated as having beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), endo-alpha-L-arabinanase (EC 3.2.1.-) as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan.
COG3533	COG3533	5.02e-42	557	1132	56	503	Uncharacterized conserved protein, DUF1680 family [Function unknown].
cd08990	GH43_AXH_like	1.55e-27	1955	2288	2	264	Glycosyl hydrolase family 43 protein, includes arabinoxylan arabinofuranohydrolase, beta-xylosidase, endo-1,4-beta-xylanase, and alpha-L-arabinofuranosidase. This subgroup includes Bacillus subtilis arabinoxylan arabinofuranohydrolase (XynD;BsAXH-m23;BSU18160), Butyrivibrio proteoclasticus alpha-L-arabinofuranosidase (Xsa43E;bpr_I2319), Clostridium stercorarium alpha-L-arabinofuranosidase XylA, and metagenomic beta-xylosidase (EC 3.2.1.37) / alpha-L-arabinofuranosidase (EC 3.2.1.55) CoXyl43. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_AXH-like subgroup includes enzymes that have been characterized with beta-xylosidase, alpha-L-arabinofuranosidase, endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. Metagenomic beta-xylosidase/alpha-L-arabinofuranosidase CoXyl43 shows synergy with Trichoderma reesei cellulases and promotes plant biomass saccharification by degrading xylo-oligosaccharides, such as xylobiose and xylotriose, into the monosaccharide xylose. Studies show that the hydrolytic activity of CoXyl43 is stimulated in the presence of calcium. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
cd09004	GH43_bXyl-like	3.67e-24	1971	2288	11	260	Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (BT3675;BT_3675) and (BT3662;BT_3662); includes mostly xylanases. This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been annotated as xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities, as well the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT88914.1	2.04e-301	1942	2592	40	690
ASB51078.1	1.06e-300	1944	2595	43	694
ALJ60075.1	2.84e-300	1942	2592	40	690
QDO68312.1	2.84e-299	1942	2593	40	691
QRQ49698.1	1.31e-290	1933	2592	31	687

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6YQH_AAA	2.44e-37	524	1143	45	574	ChainAAA, Acetyl-CoA carboxylase, biotin carboxylase [Bacteroides thetaiotaomicron VPI-5482]
5OPJ_A	5.32e-36	683	1143	152	574	Beta-L-arabinofuranosidase[Bacteroides thetaiotaomicron]
4NOV_A	6.85e-12	1955	2289	56	328	Xsa43E,a GH43 family enzyme from Butyrivibrio proteoclasticus [Butyrivibrio proteoclasticus B316]
5HO9_A	7.54e-08	302	393	548	639	Structureof truncated AbnA (domains 1-3), a GH43 arabinanase from Geobacilllus stearothermophilus, in complex with arabinooctaose [Geobacillus stearothermophilus],5HO9_B Structure of truncated AbnA (domains 1-3), a GH43 arabinanase from Geobacilllus stearothermophilus, in complex with arabinooctaose [Geobacillus stearothermophilus]
5HO0_A	8.68e-08	302	393	548	639	Crystalstructure of AbnA (closed conformation), a GH43 extracellular arabinanase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5HO2_A Crystal structure of AbnA (open conformation), a GH43 extracellular arabinanase from Geobacillus stearothermophilus [Geobacillus stearothermophilus],5HOF_A Crystal structure of AbnA, a GH43 extracellular arabinanase from Geobacillus stearothermophilus, in complex with arabinopentaose [Geobacillus stearothermophilus],5HP6_A Structure of AbnA, a GH43 extracellular arabinanase from Geobacillus stearothermophilus (a new conformational state) [Geobacillus stearothermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P48790	2.39e-28	1944	2480	7	459	Xylosidase/arabinosidase OS=Thermoclostridium stercorarium OX=1510 GN=xylA PE=1 SV=1
P33747	1.73e-17	1663	1848	18	203	Uncharacterized protein CA_P0160 OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=CA_P0160 PE=3 SV=2
P85991	2.33e-17	1720	1933	38	258	Ig-like virion protein OS=Serratia phage KSP90 OX=552528 PE=1 SV=2
P35838	3.87e-09	1683	1762	237	316	Uncharacterized protein CA_C0552 OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=CA_C0552 PE=4 SV=2
E8MGH9	4.62e-09	1218	1432	1662	1871	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

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
0.000236	0.999133	0.000167	0.000179	0.000154	0.000139

TMHMM  Annotations     

start	end
5	27