Species | CAG-1435 sp003537755 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-314; CAG-1435; CAG-1435 sp003537755 | |||||||||||
CAZyme ID | MGYG000003504_00262 | |||||||||||
CAZy Family | GH2 | |||||||||||
CAZyme Description | Beta-galactosidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 199; End: 2664 Strand: + |
MTELRLNKEW TIDYYGKQLP AVVPGDVTLD LWHNNIIDNP YFGMNHKQLH WIINRDFVYE | 60 |
TRFDVSDEIF GEQEILLEFI GINTYVDIYL NGKQLGHTQN MFLKYTYSVR DIVKKSGNLL | 120 |
IVKMLSTGRV MDSIDTRGYH GVFNVKRLFM RKAQCHFGWD WAPDMPGYGI CGDVRLVGCN | 180 |
KNRISDVHYR AFNNGKLSIF TDLNYTVREH MTEDNQLRQC SPECINDALR YIVAKRPDEP | 240 |
ISDNNCIVFE TKVSGEKNFA NFTIENPALW WPNGYGKQPL YEYKVQLVRN GKVADEYVGK | 300 |
FAFREVTLCQ QPYDQTRMQY QLQINGKNVF VKGSNWVPAE CFIGSITTEK YQRLIGQAAK | 360 |
ANFNMLRVWG GGLYEKDVFY DICDRNGIMV WQDFMFACSD IPEDDAGFVD ACQKEITYQV | 420 |
CRLRNHPSLV YWCGGNEKTG SYGLKITKGD YFVDVILRGT VDNYDGTRPY ARQSPCSLTD | 480 |
VGNDRTSGES HAGSYESSLI SGVLNYRNKV SESGVMFVSE CANMGPGTLE IYKRMFPEDK | 540 |
LWPMNEYWRD RLMENPYSEF KVPFCERQIL YADTLYGKSD TLRQFVAKGM TSHAESMRAE | 600 |
IEFARANPAC GGFMNWMYSD IWPSATWAVV DYYCEPKQAY YQMKRSYAPI VVTYVQNEDK | 660 |
RLQLVLLNDD LREVTVDVTY GMRTLDGKTV WKHTVTLTSA GGSAVDIEDK YNAPDSYLFA | 720 |
EYDMDGVKHV TVFSYDMWHT CRFASDYTYS VEKLSECYAV TIAAKQFAKG VIVRMKDNYR | 780 |
FTYSDNYVDL QAGEQITLYI YGATDKDIAT IEVTDFAKET A | 821 |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH2 | 5 | 712 | 5.5e-90 | 0.6914893617021277 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3250 | LacZ | 7.98e-52 | 6 | 704 | 15 | 688 | Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]. |
PRK10340 | ebgA | 2.35e-10 | 30 | 446 | 92 | 456 | cryptic beta-D-galactosidase subunit alpha; Reviewed |
pfam00703 | Glyco_hydro_2 | 5.66e-09 | 250 | 304 | 55 | 106 | Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities. |
PRK10150 | PRK10150 | 4.34e-06 | 55 | 452 | 61 | 429 | beta-D-glucuronidase; Provisional |
pfam17753 | Ig_mannosidase | 2.20e-04 | 748 | 812 | 5 | 68 | Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QHI68839.1 | 1.45e-173 | 1 | 819 | 1 | 829 |
AQQ71581.1 | 4.81e-166 | 19 | 798 | 38 | 812 |
AKJ63700.1 | 4.51e-131 | 19 | 798 | 28 | 821 |
ACK43074.1 | 1.69e-115 | 1 | 705 | 1 | 687 |
ACI19676.1 | 2.60e-113 | 1 | 722 | 1 | 703 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5N6U_A | 3.36e-113 | 1 | 722 | 24 | 726 | Crystalstructure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12],5N6U_B Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12],5N6U_C Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12],5N6U_D Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12] |
2VJX_A | 1.70e-95 | 6 | 692 | 11 | 696 | Structuraland biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VJX_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VL4_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VL4_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VMF_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VMF_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VO5_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VO5_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VOT_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VOT_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VQT_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VQT_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VR4_A Transition-state mimicry in mannoside hydrolysis: characterisation of twenty six inhibitors and insight into binding from linear free energy relationships and 3-D structure [Bacteroides thetaiotaomicron VPI-5482],2VR4_B Transition-state mimicry in mannoside hydrolysis: characterisation of twenty six inhibitors and insight into binding from linear free energy relationships and 3-D structure [Bacteroides thetaiotaomicron VPI-5482] |
2JE8_A | 1.77e-95 | 6 | 692 | 13 | 698 | Structureof a beta-mannosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],2JE8_B Structure of a beta-mannosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482] |
7OP6_A | 1.81e-95 | 6 | 692 | 13 | 698 | ChainA, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP6_B Chain B, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP7_A Chain A, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP7_B Chain B, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482] |
2WBK_A | 4.66e-95 | 6 | 692 | 11 | 696 | Structureof the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis [Bacteroides thetaiotaomicron VPI-5482],2WBK_B Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis [Bacteroides thetaiotaomicron VPI-5482] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
I2C092 | 1.08e-78 | 16 | 803 | 23 | 841 | Beta-mannosidase B OS=Thermothelomyces thermophilus OX=78579 GN=man9 PE=1 SV=1 |
Q95327 | 4.13e-78 | 18 | 659 | 39 | 700 | Beta-mannosidase OS=Capra hircus OX=9925 GN=MANBA PE=1 SV=1 |
Q29444 | 5.36e-77 | 18 | 659 | 39 | 700 | Beta-mannosidase OS=Bos taurus OX=9913 GN=MANBA PE=1 SV=1 |
Q4FZV0 | 8.46e-74 | 18 | 658 | 39 | 699 | Beta-mannosidase OS=Rattus norvegicus OX=10116 GN=Manba PE=2 SV=1 |
O00462 | 1.04e-72 | 18 | 659 | 39 | 700 | Beta-mannosidase OS=Homo sapiens OX=9606 GN=MANBA PE=1 SV=3 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000044 | 0.000003 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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