CAZyme Information: MGYG000004287_01464

Basic Information

• Species: Limosilactobacillus caviae
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Limosilactobacillus; Limosilactobacillus caviae
• CAZyme ID: MGYG000004287_01464
• CAZy Family: GH53
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1692	MGYG000004287_6|CGC1	185652.46	5.1553

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004287	2159846	MAG	China	Asia

• Gene Location: Start: 107416; End: 112494 Strand: +

Full Sequence      

METKRHFKLYKSGKQWITAAITTVAVSTGILMGGVANADTATPTDDQSITTTTNSSTAND
EKPEQPLKTTDLVKQDGQQENGSIEKVASKANNTDLQTSNYDHNDNGSYGAFDSVTVNDN
QLHVAGWQATNQASQYGNKNRFLIAIGHNEQGQQTELGRTKLDSQTIVARPDVKNVHNVY
NAENSGFDANIKLDVNKLQTYRNAIQIISRYSGSADGNSQYIDYVSAPVVLNRDNNAWLD
EMKVTNNQLHVSGWNATNKALGKQNHYLILFDRTLGHELSRVRVNGVARPDVEEAYPQVI
NADISGFDANFSLSNIDLTHQLQIISRYSDVTNGEGNNVNYWFAPQQLMPANPANQGSLD
QFNISKAGEVTVTGWHATDASSVENNRFLILFDQTAGHQIASLKITNVARPDVAKVYPNI
KNAQDSGFNTTFKVNPSDIIYGHQYSVVSRYSTDPNGNGNDGKHMDYWSAPITLNHSANN
IDQLGVTDKGLQISGWMASDASAKQSHAYILVMNNGKEITRQEVKLSSRPDVAKAYPSMY
NSELSGFNTTIALPNDIAQLNNLQLLLRFSTAADGNPYLNQPVTDQWSGKYNLTANEGSF
DYIKVNGSTVEVQGWHASNLSAAKPYQYLIVLKNGKEAGRSLIMGSEGKLGRPDVNRVYP
SILNSGQSGFEGSVVLANNLRNTKVQLIHRFTNDPAGNGNYVDLTSPVLTIDSNYQTGIL
NINSIRAKRDMTAQRIAQKLMAQRQAKVLYDWTNQDNNYQELAIYDIAQELAQGDVNNDA
QVIAKKLKNNALLDGKVVSTAIFDLPKTMDYDQITDNFINNIPNNSIVNNSVVGVGVANN
NLAIVLFAPGTSTATEQATSKLTAQISDVYKHAGVTVDVKNGLTKGVSVDSTDLGTALIQ
PSVMLLKGDKGTVISLDTLKTIFAALPGNTTALEGTKNYYNGNDAYHYQFWLDGQSADDK
LNNFLALNKNAKYGDQLKVNYTATLVYGSETGSNTENIDETPTSKKSADEVSLAYQNGTE
TGARYETVKVNPIPNMKQDTIRGVDVSSYLALVKNGVQFYDFNGQPADLMKVLSDAGVNY
IRIRMWVDPYNAAGESYGGGIDDEATVLQIAEDAKKYGMKVLLGLHYSDFWADPATQLVP
KQWKNLDDQDLNAEVYLYTKKLVNDFTKAGVNIDMAQLGNEITKGILGVHDEKLGANIWQ
TEPQASRITSLLSSASRAFREAAPKTQLAVHIETPDMHNYDMIMNSLKIHGVDYDVLGSS
YYPFWGWGGNNPDNIANVEKMVKDKYGKKFMIAESGWPFTLQNSDGTPNNVSWEPGHYSV
SPQGQVDEISAMYKAVLSNDNGLGAFYWEPAWIPVKAGWDNWEYNKLMGDVQGTGWASIN
SRGYYPDSKIMYQGKSASGGTSWDNNTLFDDHGYPLQSLMMYKGFLNGYQSPASVTSSFT
AKINALYKTDGVELTNPLKIGDGLDINGIFSKDGQQLLNGIENTTISDASLKAIFNDLQE
GIKSQTYTDKDGNKYHYEFWLDGNNATDKLNNFLTLNSRAKYGTPLTVNYSATLVQDEQV
EMATSFIKATVSEVYGLDGVTIDSPLKMGDSLPSTDLAVIQKAVDSALTGEKGAVISSQS
FKDLAKALPGMYGSTGALSGSKVYTMKDGNQYHYEYWLKTDDLQGANKDAKYGDPIIVTY
SASLKWIDPKTK

Enzyme Prediction     

No EC number prediction in MGYG000004287_01464.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH53	1041	1421	6.6e-109	0.9941520467836257

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3867	GanB	2.29e-94	1022	1423	21	392	Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism].
pfam07745	Glyco_hydro_53	1.18e-88	1041	1419	1	330	Glycosyl hydrolase family 53. This domain belongs to family 53 of the glycosyl hydrolase classification. These enzymes are enzymes are endo-1,4- beta-galactanases (EC:3.2.1.89). The structure of this domain is known and has a TIM barrel fold.
TIGR03715	KxYKxGKxW	3.07e-07	4	26	1	23	KxYKxGKxW signal peptide. This model describes a novel form of signal peptide that occurs as an N-terminal domain with a recognizable motif, reminiscent of the YSIRK and PEP-CTERM forms of signal peptide. This domain tends to occur on long, low-complexity (usually Serine-rich and heavily glycosylated) proteins of the Firmicutes, and (as with YSIRK) the majority of these proteins have the LPXTG cell wall-anchoring motif at the C-terminus.
NF033875	Agg_substance	0.004	1	106	5	112	LPXTG-anchored aggregation substance. Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.
cd19608	GH113_mannanase-like	0.009	1251	1397	184	302	Glycoside hydrolase family 113 beta-1,4-mannanase and similar proteins. Mannan endo-1,4-beta mannosidase (E.C 3.2.1.78) randomly cleaves (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans and is also called beta-1,4-mannanase, endo-1,4-beta-mannanase, endo-beta-1,4-mannase, beta-mannanase B, beta-1, 4-mannan 4-mannanohydrolase, endo-beta-mannanase, beta-D-mannanase, 1,4-beta-D-mannan mannanohydrolase, and 4-beta-D-mannan mannanohydrolase. (1->4)-beta-linked mannans are polysaccharides with a linear polymer backbone of (1->4)-beta-linked mannose units (in plants and fungi) or alternating mannose and glucose/galactose units (glucomannan in plants and fungi, and galactomannan and galactoglucomannan in plants), such as in the hemicellulose fraction of hard- and softwoods. Complete degradation of mannan requires a series of enzymes, including beta-1,4-mannanase. According to the CAZy database beta-1,4-mannanases are grouped into various glycoside hydrolase (GH) families; GH family 113 beta-1,4-mannanases include mostly bacterial and archaeal sequences.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QWS05217.1	0.0	1	1692	1	1708
AMY14657.1	0.0	1	1692	1	1707
AGN98817.1	0.0	1	1692	1	1707
QDK48107.1	0.0	35	1692	1	1673
QLQ61286.1	8.27e-306	729	1687	499	1471

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1R8L_A	2.54e-84	1020	1423	4	389	Thestructure of endo-beta-1,4-galactanase from Bacillus licheniformis [Bacillus licheniformis],1R8L_B The structure of endo-beta-1,4-galactanase from Bacillus licheniformis [Bacillus licheniformis],1UR0_A The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],1UR0_B The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],1UR4_A The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],1UR4_B The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],2CCR_A Structure of Beta-1,4-Galactanase [Bacillus licheniformis],2CCR_B Structure of Beta-1,4-Galactanase [Bacillus licheniformis],2J74_A Structure of Beta-1,4-Galactanase [Bacillus licheniformis],2J74_B Structure of Beta-1,4-Galactanase [Bacillus licheniformis]
2GFT_A	1.61e-83	1020	1423	4	389	ChainA, Glycosyl Hydrolase Family 53 [Bacillus licheniformis],2GFT_B Chain B, Glycosyl Hydrolase Family 53 [Bacillus licheniformis]
7OSK_A	6.66e-61	1026	1423	36	392	ChainA, Arabinogalactan endo-1,4-beta-galactosidase [Ignisphaera aggregans DSM 17230],7OSK_B Chain B, Arabinogalactan endo-1,4-beta-galactosidase [Ignisphaera aggregans DSM 17230]
1FHL_A	1.23e-40	1040	1353	3	302	CrystalStructure Of Beta-1,4-galactanase From Aspergillus Aculeatus At 293k [Aspergillus aculeatus],1FOB_A Crystal Structure Of Beta-1,4-galactanase From Aspergillus Aculeatus At 100k [Aspergillus aculeatus],6Q3R_A ASPERGILLUS ACULEATUS GALACTANASE [Aspergillus aculeatus],6Q3R_B ASPERGILLUS ACULEATUS GALACTANASE [Aspergillus aculeatus]
1HJQ_A	5.38e-40	1042	1353	5	301	Structureof two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Humicola insolens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O07013	3.40e-85	1024	1423	37	418	Endo-beta-1,4-galactanase OS=Bacillus subtilis (strain 168) OX=224308 GN=ganB PE=1 SV=1
Q65CX5	2.96e-83	1020	1423	29	414	Endo-beta-1,4-galactanase OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=ganB PE=1 SV=1
P48843	3.02e-45	1041	1373	7	337	Uncharacterized protein in bgaB 5'region (Fragment) OS=Niallia circulans OX=1397 PE=3 SV=1
A1D3T4	4.05e-41	1042	1353	26	324	Probable arabinogalactan endo-beta-1,4-galactanase A OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=galA PE=3 SV=1
Q0CTQ7	6.28e-41	1040	1352	17	316	Probable arabinogalactan endo-beta-1,4-galactanase A OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=galA PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000722	0.997765	0.000917	0.000237	0.000187	0.000148

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004287_01464.