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CAZyme Information: MGYG000002476_03941

You are here: Home > Sequence: MGYG000002476_03941

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 Yersinia pestis
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Yersinia; Yersinia pestis
CAZyme ID MGYG000002476_03941
CAZy Family AA7
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
685 MGYG000002476_3|CGC39 75270.51 6.3739
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002476 4935125 Isolate Russia Europe
Gene Location Start: 4259133;  End: 4261190  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002476_03941.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA7 17 535 7.2e-164 0.9956331877729258

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3979 COG3979 2.85e-38 542 685 5 153
Chitodextrinase [Carbohydrate transport and metabolism].
COG0277 GlcD 4.73e-16 18 538 19 459
FAD/FMN-containing dehydrogenase [Energy production and conversion].
pfam08031 BBE 9.10e-11 480 536 1 45
Berberine and berberine like. This domain is found in the berberine bridge and berberine bridge- like enzymes which are involved in the biosynthesis of numerous isoquinoline alkaloids. They catalyze the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine.
cd00063 FN3 5.81e-08 542 628 1 93
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.
cd12214 ChiA1_BD 1.12e-06 634 678 1 42
chitin-binding domain of Chi A1-like proteins. This group contains proteins related to the chitin binding domain of chitinase A1 (ChiA1) of Bacillus circulans WL-12. Glycosidase ChiA1 hydrolyzes chitin and is comprised of several domains: the C-terminal chitin binding domain, an N-terminal and catalytic domain, and 2 fibronectin type III-like domains. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source. Bacillus circulans WL-12 ChiA1 facilitates invasion of fungal cell walls. The ChiAi chitin binding domain is required for the specific recognition of insoluble chitin. although topologically and structurally related, ChiA1 lacks the characteristic aromatic residues of Erwinia chrysanthemi endoglucanase Z (CBD(EGZ)).

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AYX00436.1 0.0 1 685 1 685
VEE73860.1 0.0 1 685 1 685
AZA32001.1 0.0 1 685 1 685
AYW95221.1 0.0 1 685 1 685
AYW85797.1 0.0 1 685 1 685

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2Y08_A 2.55e-66 11 535 44 525
Structureof the substrate-free FAD-dependent tirandamycin oxidase TamL [Streptomyces sp. 307-9],2Y08_B Structure of the substrate-free FAD-dependent tirandamycin oxidase TamL [Streptomyces sp. 307-9],2Y3R_A Structure of the tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P21 space group [Streptomyces sp. 307-9],2Y3R_B Structure of the tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P21 space group [Streptomyces sp. 307-9],2Y3R_C Structure of the tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P21 space group [Streptomyces sp. 307-9],2Y3R_D Structure of the tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P21 space group [Streptomyces sp. 307-9],2Y3S_A Structure of the tirandamycine-bound FAD-dependent tirandamycin oxidase TamL in C2 space group [Streptomyces sp. 307-9],2Y3S_B Structure of the tirandamycine-bound FAD-dependent tirandamycin oxidase TamL in C2 space group [Streptomyces sp. 307-9],2Y4G_A Structure of the Tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P212121 space group [Streptomyces sp. 307-9],2Y4G_B Structure of the Tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P212121 space group [Streptomyces sp. 307-9]
2IPI_A 7.68e-64 4 535 33 517
CrystalStructure of Aclacinomycin Oxidoreductase [Streptomyces galilaeus],2IPI_B Crystal Structure of Aclacinomycin Oxidoreductase [Streptomyces galilaeus],2IPI_C Crystal Structure of Aclacinomycin Oxidoreductase [Streptomyces galilaeus],2IPI_D Crystal Structure of Aclacinomycin Oxidoreductase [Streptomyces galilaeus]
5I1V_A 1.19e-58 41 535 42 497
Crystalstructure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1V_B Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1V_C Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1V_D Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_A Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_B Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_C Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_D Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6]
2WDW_A 5.97e-54 33 535 61 521
TheNative Crystal Structure of the Primary Hexose Oxidase (Dbv29) in Antibiotic A40926 Biosynthesis [Nonomuraea gerenzanensis],2WDW_B The Native Crystal Structure of the Primary Hexose Oxidase (Dbv29) in Antibiotic A40926 Biosynthesis [Nonomuraea gerenzanensis],5AWV_A Crystal structure of glycopeptide hexose oxidase DBV29 complexed with teicoplanin [Nonomuraea gerenzanensis],5AWV_B Crystal structure of glycopeptide hexose oxidase DBV29 complexed with teicoplanin [Nonomuraea gerenzanensis],5AWV_C Crystal structure of glycopeptide hexose oxidase DBV29 complexed with teicoplanin [Nonomuraea gerenzanensis],5AWV_D Crystal structure of glycopeptide hexose oxidase DBV29 complexed with teicoplanin [Nonomuraea gerenzanensis]
3POP_A 6.54e-52 31 537 36 501
Thecrystal structure of GilR, an oxidoreductase that catalyzes the terminal step of gilvocarcin biosynthesis [Streptomyces griseoflavus],3POP_B The crystal structure of GilR, an oxidoreductase that catalyzes the terminal step of gilvocarcin biosynthesis [Streptomyces griseoflavus],3POP_C The crystal structure of GilR, an oxidoreductase that catalyzes the terminal step of gilvocarcin biosynthesis [Streptomyces griseoflavus],3POP_D The crystal structure of GilR, an oxidoreductase that catalyzes the terminal step of gilvocarcin biosynthesis [Streptomyces griseoflavus],3PQB_A The crystal structure of pregilvocarcin in complex with GilR, an oxidoreductase that catalyzes the terminal step of gilvocarcin biosynthesis [Streptomyces griseoflavus],3PQB_B The crystal structure of pregilvocarcin in complex with GilR, an oxidoreductase that catalyzes the terminal step of gilvocarcin biosynthesis [Streptomyces griseoflavus],3PQB_C The crystal structure of pregilvocarcin in complex with GilR, an oxidoreductase that catalyzes the terminal step of gilvocarcin biosynthesis [Streptomyces griseoflavus],3PQB_D The crystal structure of pregilvocarcin in complex with GilR, an oxidoreductase that catalyzes the terminal step of gilvocarcin biosynthesis [Streptomyces griseoflavus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A3RXB7 1.62e-122 11 535 12 506
N-acetyl-D-hexosamine oxidase OS=Ralstonia solanacearum (strain UW551) OX=342110 GN=RRSL_02030 PE=1 SV=1
P93762 1.41e-81 3 536 13 535
Hexose oxidase OS=Chondrus crispus OX=2769 GN=HOX PE=1 SV=2
Q0PCD7 7.14e-63 4 535 57 541
Aclacinomycin-N/aclacinomycin-A oxidase OS=Streptomyces galilaeus OX=33899 GN=aknOx PE=1 SV=1
Q796Y5 1.61e-27 2 536 9 443
Uncharacterized FAD-linked oxidoreductase YgaK OS=Bacillus subtilis (strain 168) OX=224308 GN=ygaK PE=3 SV=4
Q5QJ60 1.47e-25 27 536 75 519
Berberine bridge enzyme-like Cyn d 4 OS=Cynodon dactylon OX=28909 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
1.000043 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002476_03941.