CAZyme Information: MGYG000004116_01341

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; UMGS1591
• CAZyme ID: MGYG000004116_01341
• CAZy Family: GH51
• CAZyme Description: Intracellular exo-alpha-(1->5)-L-arabinofuranosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
500	MGYG000004116_6|CGC3	56371.84	5.6868

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004116	3787047	MAG	United Kingdom	Europe

• Gene Location: Start: 99434; End: 100936 Strand: -

Full Sequence      

MKASLTLCRDYVIGEVDPRLFGSFVEHMGRCVYGGIYEPGHPSADNWGFRGDVLSLVREL
QVPIIRYPGGNFVSGYNWEDGTGPREKRPRRADLAWRTVETNQVGIDEFQEWARRAGTEV
MMAVNLGTRGPEDAKNLVEYCNHPGGTAESDRRIANGFKAPFGIRTWCLGNEMDGPWQTC
AKSAAEYGRIAREAAKMMKRVDPSIELVACGSSYRAMPTFGRWESAVLDELYEEVDYLSM
HSYYGNHTGDTSAYLASSLDMEACIRAQIAVCDHMQAVKRAKKTLHLSYDEWNVWYRTGE
TDIQPWQTAPPLLEEDYNLEDALVAGTLLTTLLRHADRVKIACLAQLVNVIAPIRTRTGG
GVWKQTIYYPYLHASLYGRGISLLPALRCGGYETREYGQVPYLECAAVWREEEGELTVMA
VNRSLDEALELELDLRDFPGLKICRHILLTHKDVQAGNTEAEPDKVVPQERENLLSGGRE
RATLPPRSWNVLRYCRKQAD

Enzyme Prediction     

EC	3.2.1.55

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH51	2	498	3.8e-136	0.7333333333333333

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3534	AbfA	0.0	1	493	2	497	Alpha-L-arabinofuranosidase [Carbohydrate transport and metabolism].
pfam06964	Alpha-L-AF_C	9.05e-78	290	488	1	192	Alpha-L-arabinofuranosidase C-terminal domain. This family represents the C-terminus (approximately 200 residues) of bacterial and eukaryotic alpha-L-arabinofuranosidase (EC:3.2.1.55). This catalyzes the hydrolysis of nonreducing terminal alpha-L-arabinofuranosidic linkages in L-arabinose-containing polysaccharides.
smart00813	Alpha-L-AF_C	8.75e-65	290	488	1	189	Alpha-L-arabinofuranosidase C-terminus. This entry represents the C terminus (approximately 200 residues) of bacterial and eukaryotic alpha-L-arabinofuranosidase. This catalyses the hydrolysis of non-reducing terminal alpha-L-arabinofuranosidic linkages in L-arabinose-containing polysaccharides.
cd12173	PGDH_4	0.007	187	241	146	199	Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains. Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AMQ20687.1	7.04e-232	2	493	5	498
QOR82949.1	1.94e-231	2	493	5	498
AGE22472.1	2.75e-231	2	493	5	498
QKI81458.1	3.07e-231	2	493	5	498
AGT32226.1	4.05e-231	2	493	5	498

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1PZ3_A	4.63e-229	2	493	5	498	Crystalstructure of a family 51 (GH51) alpha-L-arabinofuranosidase from Geobacillus stearothermophilus T6 [Geobacillus stearothermophilus],1PZ3_B Crystal structure of a family 51 (GH51) alpha-L-arabinofuranosidase from Geobacillus stearothermophilus T6 [Geobacillus stearothermophilus],6SXU_AAA Chain AAA, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Geobacillus stearothermophilus],6SXU_BBB Chain BBB, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Geobacillus stearothermophilus],6SXV_A GH51 a-l-arabinofuranosidase soaked with aziridine inhibitor [Geobacillus stearothermophilus],6SXV_B GH51 a-l-arabinofuranosidase soaked with aziridine inhibitor [Geobacillus stearothermophilus]
1PZ2_A	3.77e-228	2	493	5	498	ChainA, Alpha-L-arabinofuranosidase [Geobacillus stearothermophilus],1PZ2_B Chain B, Alpha-L-arabinofuranosidase [Geobacillus stearothermophilus],1QW8_A Chain A, Alpha-L-arabinofuranosidase [Geobacillus stearothermophilus],1QW8_B Chain B, Alpha-L-arabinofuranosidase [Geobacillus stearothermophilus],1QW9_A Chain A, Alpha-L-arabinofuranosidase [Geobacillus stearothermophilus],1QW9_B Chain B, Alpha-L-arabinofuranosidase [Geobacillus stearothermophilus]
5O7Z_A	3.63e-199	2	493	2	499	ChainA, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O7Z_B Chain B, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O7Z_C Chain C, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O7Z_D Chain D, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O7Z_E Chain E, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O7Z_F Chain F, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O80_A Chain A, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O80_B Chain B, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O80_C Chain C, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O80_D Chain D, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O80_E Chain E, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O80_F Chain F, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila]
2C7F_A	5.53e-199	2	493	13	510	ChainA, Alpha-l-arabinofuranosidase [Acetivibrio thermocellus],2C7F_B Chain B, Alpha-l-arabinofuranosidase [Acetivibrio thermocellus],2C7F_C Chain C, Alpha-l-arabinofuranosidase [Acetivibrio thermocellus],2C7F_D Chain D, Alpha-l-arabinofuranosidase [Acetivibrio thermocellus],2C7F_E Chain E, Alpha-l-arabinofuranosidase [Acetivibrio thermocellus],2C7F_F Chain F, Alpha-l-arabinofuranosidase [Acetivibrio thermocellus],2C8N_A Chain A, ALPHA-L-ARABINOFURANOSIDASE [Acetivibrio thermocellus],2C8N_B Chain B, ALPHA-L-ARABINOFURANOSIDASE [Acetivibrio thermocellus],2C8N_C Chain C, ALPHA-L-ARABINOFURANOSIDASE [Acetivibrio thermocellus],2C8N_D Chain D, ALPHA-L-ARABINOFURANOSIDASE [Acetivibrio thermocellus],2C8N_E Chain E, ALPHA-L-ARABINOFURANOSIDASE [Acetivibrio thermocellus],2C8N_F Chain F, ALPHA-L-ARABINOFURANOSIDASE [Acetivibrio thermocellus]
5O81_A	2.96e-198	2	493	2	499	ChainA, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O81_B Chain B, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O81_C Chain C, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O81_D Chain D, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O81_E Chain E, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O81_F Chain F, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O82_A Chain A, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O82_B Chain B, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O82_C Chain C, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O82_D Chain D, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O82_E Chain E, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila],5O82_F Chain F, Intracellular exo-alpha-(1->5)-L-arabinofuranosidase [Thermochaetoides thermophila]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9XBQ3	2.53e-228	2	493	5	498	Intracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Geobacillus stearothermophilus OX=1422 GN=abfA PE=1 SV=4
Q9KBR4	3.35e-216	1	497	3	500	Intracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) OX=272558 GN=abfA PE=3 SV=1
P94531	6.90e-211	2	493	3	495	Intracellular exo-alpha-(1->5)-L-arabinofuranosidase 1 OS=Bacillus subtilis (strain 168) OX=224308 GN=abfA PE=1 SV=2
A3DIH0	2.62e-199	2	493	3	500	Intracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=Cthe_2548 PE=1 SV=1
P53627	3.85e-182	3	493	4	499	Intracellular exo-alpha-(1->5)-L-arabinofuranosidase OS=Streptomyces lividans OX=1916 GN=abfA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000045	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004116_01341.