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CAZyme Information: MGYG000000198_00536

You are here: Home > Sequence: MGYG000000198_00536

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Enterocloster citroniae
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Enterocloster; Enterocloster citroniae
CAZyme ID MGYG000000198_00536
CAZy Family GH42
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
697 MGYG000000198_1|CGC7 80076.5 4.7169
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000198 6476049 Isolate China Asia
Gene Location Start: 572721;  End: 574814  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000198_00536.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH42 26 395 2.4e-45 0.9703504043126685
GH164 219 692 1e-15 0.7194029850746269

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam08532 Glyco_hydro_42M 4.66e-18 439 592 30 189
Beta-galactosidase trimerisation domain. This is non catalytic domain B of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. This domain is related to glutamine amidotransferase enzymes, but the catalytic residues are replaced by non functional amino acids. This domain is involved in trimerisation.
COG1874 GanA 1.12e-17 9 586 11 585
Beta-galactosidase GanA [Carbohydrate transport and metabolism].
pfam02449 Glyco_hydro_42 1.67e-16 20 396 2 376
Beta-galactosidase. This group of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. The enzyme catalyzes the hydrolysis of terminal, non-reducing terminal beta-D-galactosidase residues.
cd03143 A4_beta-galactosidase_middle_domain 1.80e-10 439 519 26 105
A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to beta-galactosidase from Thermus thermophilus. Beta-Galactosidase hydrolyzes the beta-1,4-D-galactosidic linkage of lactose, as well as those of related chromogens, o-nitrophenyl-beta-D-galactopyranoside (ONP-Gal) and 5-bromo-4-chloro-3-indolyl-beta-D-galactoside (X-gal). This A4 beta-galactosidase middle domain lacks the catalytic triad of typical GATase1 domains. The reactive Cys residue found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow in typical GATase1 domains is not conserved in this group.
pfam07090 GATase1_like 0.002 554 589 181 217
Putative glutamine amidotransferase. This family consists of several hypothetical bacterial proteins of around 250 residues in length. The function of this family is unknown. The structure of this cytoplasmic domain was solved by the Midwest Center for Structural Genomics (MCSG). The structure has been classified as part of the Class-I Glutamine amidotransferase superfamily owing to similarity with other known structures. The monomer combines with itself to form a hexamer, and this hexamer exposes a potential catalytic surface rich in Glu, Asp, Tyr, Ser.Trp and His residues.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QDS99940.1 4.61e-205 15 692 5 684
AHF91909.1 1.55e-169 16 652 13 671
QGQ98429.1 1.51e-75 12 645 2 650
QYY35048.1 9.66e-59 12 665 11 671
AQQ71006.1 1.12e-42 14 589 2 588

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4UNI_A 1.94e-16 16 603 25 620
beta-(1,6)-galactosidasefrom Bifidobacterium animalis subsp. lactis Bl-04 in complex with galactose [Bifidobacterium animalis subsp. lactis Bl-04],4UNI_B beta-(1,6)-galactosidase from Bifidobacterium animalis subsp. lactis Bl-04 in complex with galactose [Bifidobacterium animalis subsp. lactis Bl-04],4UNI_C beta-(1,6)-galactosidase from Bifidobacterium animalis subsp. lactis Bl-04 in complex with galactose [Bifidobacterium animalis subsp. lactis Bl-04]
4UOQ_A 1.02e-15 16 603 25 620
Nucleophilemutant (E324A) of beta-(1,6)-galactosidase from Bifidobacterium animalis subsp. lactis Bl-04 [Bifidobacterium animalis subsp. lactis Bl-04],4UOQ_B Nucleophile mutant (E324A) of beta-(1,6)-galactosidase from Bifidobacterium animalis subsp. lactis Bl-04 [Bifidobacterium animalis subsp. lactis Bl-04],4UOQ_C Nucleophile mutant (E324A) of beta-(1,6)-galactosidase from Bifidobacterium animalis subsp. lactis Bl-04 [Bifidobacterium animalis subsp. lactis Bl-04],4UOZ_A beta-(1,6)-galactosidase from Bifidobacterium animalis subsp. lactis Bl-04 nucleophile mutant E324A in complex with galactose [Bifidobacterium animalis subsp. lactis Bl-04],4UOZ_B beta-(1,6)-galactosidase from Bifidobacterium animalis subsp. lactis Bl-04 nucleophile mutant E324A in complex with galactose [Bifidobacterium animalis subsp. lactis Bl-04],4UOZ_C beta-(1,6)-galactosidase from Bifidobacterium animalis subsp. lactis Bl-04 nucleophile mutant E324A in complex with galactose [Bifidobacterium animalis subsp. lactis Bl-04]
3TTS_A 3.65e-14 125 632 117 630
ChainA, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTS_B Chain B, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTS_C Chain C, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTS_D Chain D, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTS_E Chain E, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTS_F Chain F, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTY_A Chain A, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTY_B Chain B, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTY_C Chain C, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTY_D Chain D, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTY_E Chain E, Beta-galactosidase [Niallia circulans subsp. alkalophilus],3TTY_F Chain F, Beta-galactosidase [Niallia circulans subsp. alkalophilus]
4UCF_A 3.70e-11 16 592 22 605
Crystalstructure of Bifidobacterium bifidum beta-galactosidase in complex with alpha-galactose [Bifidobacterium bifidum S17],4UCF_B Crystal structure of Bifidobacterium bifidum beta-galactosidase in complex with alpha-galactose [Bifidobacterium bifidum S17],4UCF_C Crystal structure of Bifidobacterium bifidum beta-galactosidase in complex with alpha-galactose [Bifidobacterium bifidum S17],4UZS_A Crystal structure of Bifidobacterium bifidum beta-galactosidase [Bifidobacterium bifidum S17],4UZS_B Crystal structure of Bifidobacterium bifidum beta-galactosidase [Bifidobacterium bifidum S17],4UZS_C Crystal structure of Bifidobacterium bifidum beta-galactosidase [Bifidobacterium bifidum S17]
6LVW_A 3.64e-08 17 630 4 635
PolyextremophilicBeta-galactosidase from the Antarctic haloarchaeon Halorubrum lacusprofundi [Halorubrum lacusprofundi ATCC 49239]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9KI47 1.25e-14 125 611 118 613
Beta-galactosidase BgaA OS=Planococcus sp. (strain 'SOS Orange') OX=128803 GN=bgaA PE=1 SV=1
C8WV58 3.86e-14 14 586 14 591
Beta-galactosidase BglY OS=Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-IA) OX=521098 GN=bglY PE=1 SV=1
D5JGG0 1.13e-13 14 632 8 619
Beta-galactosidase LacZ OS=Weizmannia coagulans OX=1398 GN=lacZ PE=3 SV=1
D4QFE7 2.03e-10 16 592 22 605
Beta-galactosidase BbgII OS=Bifidobacterium bifidum OX=1681 GN=bbgII PE=3 SV=1
Q9RFN0 1.63e-08 125 610 115 598
Beta-galactosidase BgaB OS=Carnobacterium maltaromaticum OX=2751 GN=bgaB PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000070 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000198_00536.