CAZyme Information: MGYG000001063_05442

Basic Information

• Species: Robinsoniella sp900540475
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Robinsoniella; Robinsoniella sp900540475
• CAZyme ID: MGYG000001063_05442
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1827		201702.93	5.0676

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001063	7637037	MAG	Sweden	Europe

• Gene Location: Start: 74926; End: 80409 Strand: +

Full Sequence      

MKRKNGFARGVSFMLSMALVLNTIVMPVSASGQNGAAQVSAGGQVLEIEYEQAEKRGTET
EINQPVRDAAAAAQQADAEMENNSDTGIDSDSGIGTDTGIDTETGTNFVTEAEIDSEKVT
EADTETELNGGQEIITEKEKDIDAATVTEKESGLDQEPESVTGENTVKALTDMEIGLFGE
IFNTEGYRGGSMELFNFENKTGEQVFASLSGQNLRPVFDKYNGNKGDEQFATARFTGKLN
VEKAGDYKFFGWGDDGFRIWIDGKLVIDFWVQEWEKEQTSKAVALSEGLHDIKIEYLQGW
GGAVLKLSWESANANIAKEVIPEKAFYHAKTPADTGLTAQIYKVNGKPSSITSFGFAGEP
VNQVLPNLDGHDGLKEAIQLSNGSSEYATAIIHGYITPQESGDYEFVMSGDDAFRFWMKD
EMMVNSWKLHSDQTKVSQPVHMEKGFLYKIRINYAQADGDANLNLSWKKDGGQAQVVPAE
CFRQAAKAIQGETAAEDQHGLLAEVYGDIFLEEKKGEVIAPVLDKSLSIKKILSQYNGSE
EYGSFRFTGQVNAEEAGDYTFYLIGDDGFRLWVNDELAIDFWESKWDKQQESQPIHLNEG
RNDIRIEYFQGFGGAYIMLEWLKPGAEEKEVIPTENLYPASTKKGLIGEIYQEKGGNQEK
LAEVLANEVSSEQFSVNSLVSYYEGNENAPANVELNGKIKPEVSGTYEFAFGSSGNYQVY
LNDEKIISQNAGNVYKETQSAKVELEKGIYYNLTIIAENLNLKEDINLSWTRDGVKSVIG
EDQLYAPEAMWYESVTAREKLYVGLTEAVALRRNTKVGSGEGQIAKEHMDKFSAVVDEIA
ADAKDFDIIASVLKEDTNKITDAVAEFKLNVIRVQKGEALTQFNNGLYQGQDPFISYHDG
YYYFVSSSNDPSHNKMYVSKSKSLLDQGEKVRIFDFNDSKSRIFAPEMFFIDGKWYIYYC
ADAKEYNWRHMACVMESVTDDPQGDWIDRGVLYTGMEIHNPNEFAQGNDFTVFQYRGQLY
ACWGSMESGVESPAIARMESPIKITEERSFLPGFGGEGPRAVVNGDHLFMTVSQGSFKTA
GYHMGMYIFDTAKDDLLNPDNWSYKEGVFEGTKDVYGPARASFFKSADGTEDWMAFHSKV
YPSNNNAWRQVSIKKITWNEDGSPNFGRPVSPYEFTALPSGDPGLGLAYQAEDGDLSGGA
KKGYKGKGFQGTGYGNITDTLGEKVTFNVNAPADGDYFVRARYANGVKAPISATDNRGEW
EANIPDITPKAGTLNLYVNDAGQKSVTVSFDKTETDWQHWMTVCSRVTLKKGENTISYVK
DAENSGNVYLDYITVQEAHEQPAAQTVKTGAELDALIAEVEGFRQEAYSIETWRIFSAAL
LSAKSVNKNAVQAVSNRYLSLEAAAKDLSNYVRFHADKNVSVSGDVKDDMYRIGSEVTVQ
AKDLAGKTFSRWDVSGFELTEEQKVSKEFTFTVPRNRGSIVPVYAENEYYKVTAGTNVRI
DNAAANSLYQAGTTVKATVEIPQGKEFIGWDVKGITLTEAEKMAVTISFVMPESEVVLNA
VFKNIVIPEKPKYQLKAGAGISIANAAKDQMYTAGTRIQATVSVPAGKVFVQWKVSGISL
TAQQQKSTVISFLMPASSVSLEAVFDIQKKKQTITAKDFQKTDGDKSFYIKAKASGKGKL
SYKSDHTKVVKVDSKGKVTIKGTGKAQITITAAGNSSYDSAIKKITISVAPKKTADVKAV
SKKSKTLKLTWKKTRGASGYLISYSTDKKFKKGVKKVVISSGKTTSRTIKNLKGKKTCYV
KVRAFKTSGKSRVYGKYSKTVSVRVKK

Enzyme Prediction     

No EC number prediction in MGYG000001063_05442.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	883	1164	4.6e-61	0.9965986394557823

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18820	GH43_LbAraf43-like	2.61e-74	891	1139	1	258	Glycosyl hydrolase family 43 proteins similar to Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans GbtXyl43B. This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes enzymes with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55) and possibly bifunctional xylosidase/arabinofuranosidase activities, similar to Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans IT-08 beta-xylosidase / exo-xylanase (GbtXyl43B). 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.
cd08980	GH43_LbAraf43-like	1.52e-40	892	1137	2	274	Glycosyl hydrolase family 43 proteins such as Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans GbtXyl43B. This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55) and possibly bifunctional xylosidase/arabinofuranosidase activities. In addition to Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43 and Geobacillus thermoleovorans IT-08 beta-xylosidase / exo-xylanase (GbtXyl43B). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) familiesGH43 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.
cd18817	GH43f_LbAraf43-like	3.20e-40	892	1139	2	262	Glycosyl hydrolase family 43 such as Lactobacillus brevis alpha-L-arabinofuranosidase LbAraf43. This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with alpha-L-arabinofuranosidase (EC 3.2.1.55) activity. 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. Characterized enzymes belonging to this subgroup include Lactobacillus brevis (LbAraf43) and Weissella sp (WAraf43) which show activity with similar catalytic efficiency on 1,5-alpha-L-arabinooligosaccharides with a degree of polymerization (DP) of 2-3; size is limited by an extended loop at the entrance to the active site. 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.
COG3940	COG3940	4.24e-38	889	1169	12	313	Beta-xylosidase, GH43 family [Carbohydrate transport and metabolism].
pfam04616	Glyco_hydro_43	2.87e-30	892	1164	12	281	Glycosyl hydrolases family 43. The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyze the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. 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
ASK62305.1	9.38e-159	499	1338	34	722
QJE96570.1	2.60e-102	881	1338	24	466
QLG40883.1	8.91e-52	883	1339	36	466
AIQ73224.1	1.56e-51	883	1336	35	462
AYB42892.1	1.80e-50	883	1339	35	465

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6QE7_A	1.15e-29	394	638	52	289	ChainA, Anti-sigma-I factor RsgI3 [Acetivibrio thermocellus],6QE7_B Chain B, Anti-sigma-I factor RsgI3 [Acetivibrio thermocellus],6QE7_C Chain C, Anti-sigma-I factor RsgI3 [Acetivibrio thermocellus]
5M8B_A	9.39e-29	878	1175	23	345	ChainA, Alpha-L-arabinofuranosidase II [Levilactobacillus brevis],5M8B_B Chain B, Alpha-L-arabinofuranosidase II [Levilactobacillus brevis]
6QDI_A	1.01e-26	394	639	51	294	ChainA, PA14 domain-containing protein [Acetivibrio clariflavus]
3AKF_A	7.43e-26	892	1171	21	317	Crystalstructure of exo-1,5-alpha-L-arabinofuranosidase [Streptomyces avermitilis MA-4680 = NBRC 14893],3AKG_A Crystal structure of exo-1,5-alpha-L-arabinofuranosidase complexed with alpha-1,5-L-arabinofuranobiose [Streptomyces avermitilis MA-4680 = NBRC 14893],3AKH_A Crystal structure of exo-1,5-alpha-L-arabinofuranosidase complexed with alpha-1,5-L-arabinofuranotriose [Streptomyces avermitilis MA-4680 = NBRC 14893],3AKI_A Crystal structure of exo-1,5-alpha-L-arabinofuranosidase complexed with alpha-L-arabinofuranosyl azido [Streptomyces avermitilis MA-4680 = NBRC 14893]
5M8E_A	3.31e-24	884	1175	27	343	Crystalstructure of a GH43 arabonofuranosidase from Weissella sp. strain 142 [Weissella cibaria],5M8E_B Crystal structure of a GH43 arabonofuranosidase from Weissella sp. strain 142 [Weissella cibaria]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A3DC75	7.96e-27	394	638	405	642	Anti-sigma-I factor RsgI3 OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=rsgI3 PE=1 SV=1
Q82P90	4.73e-25	892	1171	47	343	Extracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680) OX=227882 GN=Araf43A PE=1 SV=1
P82594	2.47e-23	889	1141	57	321	Extracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Streptomyces chartreusis OX=1969 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
0.000384	0.998864	0.000247	0.000170	0.000162	0.000149

TMHMM  Annotations     

start	end
7	29