dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

RUG572 sp900547945

Lineage

Bacteria; Verrucomicrobiota; Kiritimatiellae; RFP12; UBA1067; RUG572; RUG572 sp900547945

CAZyme ID

MGYG000003483_00398

CAZy Family

GH5

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
824		90701.06	8.7694

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003483	3685575	MAG	Fiji	Oceania

Gene Location

Start: 7526; End: 10000 Strand: +

Enzyme Prediction help

No EC number prediction in MGYG000003483_00398.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH5	192	465	4.5e-44	0.7454545454545455

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00150	Cellulase	3.73e-21	194	456	27	271	Cellulase (glycosyl hydrolase family 5).
COG2730	BglC	1.73e-18	192	468	74	374	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
cd00408	DHDPS-like	1.78e-07	504	754	2	238	Dihydrodipicolinate synthase family. Dihydrodipicolinate synthase family. A member of the class I aldolases, which use an active-site lysine which stabilizes a reaction intermediate via Schiff base formation, and have TIM beta/alpha barrel fold. The dihydrodipicolinate synthase family comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways and includes such proteins as N-acetylneuraminate lyase, MosA protein, 5-keto-4-deoxy-glucarate dehydratase, trans-o-hydroxybenzylidenepyruvate hydratase-aldolase, trans-2'-carboxybenzalpyruvate hydratase-aldolase, and 2-keto-3-deoxy- gluconate aldolase. The family is also referred to as the N-acetylneuraminate lyase (NAL) family.
COG0329	DapA	6.84e-05	606	812	102	299	Dihydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and metabolism, Cell wall/membrane/envelope biogenesis].
cd00950	DHDPS	0.001	617	702	110	201	Dihydrodipicolinate synthase (DHDPS). Dihydrodipicolinate synthase (DHDPS) is a key enzyme in lysine biosynthesis. It catalyzes the aldol condensation of L-aspartate-beta- semialdehyde and pyruvate to dihydropicolinic acid via a Schiff base formation between pyruvate and a lysine residue. The functional enzyme is a homotetramer consisting of a dimer of dimers. DHDPS is member of dihydrodipicolinate synthase family that comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AVM45719.1	1.51e-144	25	495	73	550
AVM46198.1	2.70e-142	26	496	28	501
AVM44768.1	7.72e-131	24	494	36	509
AVM45721.1	3.53e-127	38	494	58	513
AVM46390.1	4.79e-127	24	496	25	503

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1CEC_A	1.90e-22	231	476	63	332	ChainA, ENDOGLUCANASE CELC [Acetivibrio thermocellus]
1CEN_A	4.64e-22	231	476	63	332	ChainA, CELLULASE CELC [Acetivibrio thermocellus],1CEO_A Chain A, CELLULASE CELC [Acetivibrio thermocellus]
3AMC_A	5.27e-15	189	458	31	288	Crystalstructures of Thermotoga maritima Cel5A, apo form and dimer/au [Thermotoga maritima MSB8],3AMC_B Crystal structures of Thermotoga maritima Cel5A, apo form and dimer/au [Thermotoga maritima MSB8],3AMD_A Crystal structures of Thermotoga maritima Cel5A, apo form and tetramer/au [Thermotoga maritima MSB8],3AMD_B Crystal structures of Thermotoga maritima Cel5A, apo form and tetramer/au [Thermotoga maritima MSB8],3AMD_C Crystal structures of Thermotoga maritima Cel5A, apo form and tetramer/au [Thermotoga maritima MSB8],3AMD_D Crystal structures of Thermotoga maritima Cel5A, apo form and tetramer/au [Thermotoga maritima MSB8],3MMU_A Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_B Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_C Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_D Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_E Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_F Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_G Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_H Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMW_A Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMW_B Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMW_C Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMW_D Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima]
3AZR_A	3.08e-14	189	458	31	288	DiverseSubstrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Cellobiose [Thermotoga maritima MSB8],3AZR_B Diverse Substrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Cellobiose [Thermotoga maritima MSB8],3AZS_A Diverse Substrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Mannotriose [Thermotoga maritima MSB8],3AZS_B Diverse Substrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Mannotriose [Thermotoga maritima MSB8],3AZT_A Diverse Substrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Cellotetraose [Thermotoga maritima MSB8],3AZT_B Diverse Substrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Cellotetraose [Thermotoga maritima MSB8],3AZT_C Diverse Substrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Cellotetraose [Thermotoga maritima MSB8],3AZT_D Diverse Substrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Cellotetraose [Thermotoga maritima MSB8]
3AMG_A	3.08e-14	189	458	31	288	Crystalstructures of Thermotoga maritima Cel5A in complex with Cellobiose substrate, mutant form [Thermotoga maritima MSB8],3AMG_B Crystal structures of Thermotoga maritima Cel5A in complex with Cellobiose substrate, mutant form [Thermotoga maritima MSB8]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A3DJ77	7.71e-22	231	476	63	332	Endoglucanase C OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celC PE=3 SV=1
P23340	7.71e-22	231	476	63	332	Endoglucanase C307 OS=Clostridium sp. (strain F1) OX=1508 GN=celC307 PE=1 SV=1
P0C2S3	1.89e-21	231	476	63	332	Endoglucanase C OS=Acetivibrio thermocellus OX=1515 GN=celC PE=1 SV=1
P14250	6.43e-11	192	380	340	521	Endoglucanase 3 OS=Fibrobacter succinogenes (strain ATCC 19169 / S85) OX=59374 GN=cel-3 PE=1 SV=2
P54583	8.13e-09	236	454	135	363	Endoglucanase E1 OS=Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) OX=351607 GN=Acel_0614 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000466	0.998353	0.000632	0.000196	0.000172	0.000164

TMHMM Annotations help

There is no transmembrane helices in MGYG000003483_00398.

You are here: Home > Sequence: MGYG000003483_00398