CAZyme Information: MGYG000004203_01380

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Acetatifactor
• CAZyme ID: MGYG000004203_01380
• CAZy Family: GH5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1948	MGYG000004203_10|CGC1	211380.31	4.289

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004203	2860639	MAG	United Kingdom	Europe

• Gene Location: Start: 66891; End: 72737 Strand: -

Full Sequence      

MKGKKVLGILLSLTMIVTGLPGMGQAAVVKAGSGTVSGGNGTVSDGDSTVSGGDEDIMLY
SGEIPDFNTVFEHYVTVDGTRLMDGDKELKFVSLNYPQATSDTAWEAANAVKTIKAMGGN
VTRSYTIPVYNGQNSAKAYVTGVDSNGNLTFNENALQSLDNLLAVCNQYGVRLIIPLVDH
WHWIGGMDGYVWLAGEADGTPSQSGFQDWAWKFYSSDKCKDYFKQMISHLLERENSVTGI
KYKDDPAILCWETGNELGNRQQEEKDQILFDWTNEVVDHIKGIDQNHLVLDGRMSMSTLS
VTAGNKADILGAHYYEGNYAERCAADTQKAHAAGKPFILGEFGAKVEAQPCIDVFQKGLE
NNTNGIMMWSLRAHKDGFGYYFHDEDGFWAAYHWPGFPSGSYYGETEILRALYAYAQIAN
GKAVTYEEAKNIPIPAPETDEAPLLYGDGSYHNSFKDGSVGDIKWRGVVGGAWYEIQRAD
GTVSEENAGLAEWQTIADEQDYVYDSGRNWEDKAHDCIAGFHDETAIDGQAYSYRLRACN
ESGVGLWSNIVTVGAAKHVVEDDLDLIAVSSTDANPTEVRNTYSSDHSANITYSSSSVVN
QSTTEGYIEYEAIIPVSEVVVTALSETEEGSTPKICVSADGINFTPVTVDHAAGTKTYSA
AGVSTAEKYYYTRIYIAGESKSKLDSVTITYMNDGNSYRGENEGGTVKTNVMIQDNKFGI
GAEPQYITKSANLAAADGAVKGITPNDGQAASILYKTGDDINAYRIVACCKDGAEPVVEY
SYDGVSYERSGVLAETTENGYTKITYGDLNVVDTIRVIRISFPADSQNKVILKSVELSSG
TKSIPLSESAPENTIEDGEYYFGDNDNLKAEYHIEKDGNSLVYSKELGKADFSGYDSIYA
WVKPDVANNTVYVDSVYAGSSTKADDFEGYSGSNNLLNAAYSRNSGGGAFNMSLDTHHKS
EGTYGARIDYDYEGKGYAGAVKEMDMLNLQGYDGFMMYLESDGSGNQFKLQMRTNKSTYN
YTGYLTGKGPMTYYLPFRDIIEADWTGGSSPLDESQNLLTVELYTNQEGSVTKGTFYVDD
IKGANFVTDLESETKVTLDMPANGGMVQAFPYVISGTAKYVDYISVTVGEKVFNVPVNAD
GTWAYELTADSGVFNGTDIAVKAGFYYPNKTAIAETGETTITVDVTGNDAPVVESYDIVA
WDWDFAADGTEGWTFTGFTPWVENENLVAWTQTAYSATFSYTVTGIPNGVYTLQNDIKVK
SNMNNVQIALGDGSSEVKSAPIDTQDVLEQNLFLGKKFEVTNHRLTLIYYVDAPTDANGA
TFAVGNIKLYLAESNDLIQNGSFTDTEPHTGGWPNYPKEWTVEPYTGSGDIKTESSWYEA
DNNKVMVVTAGTAFRIAQDVVISDIDAGTYELSALIDTAHNNAAVSDFVMKVTDDGGKEV
ASVALADGTCKIPDMELAAGTYTVSLSGTLESGTVYLDDVSLVLNAWAQRTPAVVNYVEN
GDFADVETDWPNLPKIWSTAYTGGDGWSPIKTQAADADNVFVGYADSAYTFTLSQDVANL
PDGTYKLSADVKLLNADTINSFVMKAGSKTLDLKPLLVADTVKKVSLGDITVTGGTLTIG
FEADFIQKGVQIDNVLLTQTDAGNGSSSLSETGGRGVIRVLNAPANVQTTGTLTNSGELK
LYLQLVDGSGKTWISNGVALTGTKGGMNKFAFDSNAEIDFTSVKEFRFVIQSSKELESAS
GEVSLSDKNCYTGNYGVALKYEISESQNSGGSDEPGGNTGEGGDKNPDKPNQDDKPNPDE
KPNPDNQPGGENKPSGGNTQNTASSGNHQSTGTTASEKEDRRVEIQYVVVRGDTLSRIAH
RYGISLAELLAANPQIKNPNRIYPGQVITIGYAQKDDSDEAFYYIIRRGDTLLRIARSHK
IPYQQLRMLNPQIVRQRYIYPGQRLRIR

Enzyme Prediction     

No EC number prediction in MGYG000004203_01380.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	109	376	1.5e-70	0.9765625
CBM23	925	1082	1.4e-33	0.9691358024691358

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00118	LysM	1.02e-14	1845	1890	1	45	Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
PRK06347	PRK06347	5.82e-14	1813	1947	306	449	1,4-beta-N-acetylmuramoylhydrolase.
smart00257	LysM	2.67e-13	1847	1890	2	44	Lysin motif.
TIGR02899	spore_safA	3.21e-13	1849	1890	1	42	spore coat assembly protein SafA. SafA (YrbB) (SafA) of Bacillus subtilis is a protein found at the interface of the spore cortex and spore coat, and is dependent on SpoVID for its localization. This model is based on the N-terminal LysM (lysin motif) domain (see pfamAM model pfam01476) of SafA and, from several other spore-forming species, the protein with the most similar N-terminal region. However, this set of proteins differs greatly in C-terminal of the LysM domaim; blocks of 12-residue and 13-residue repeats are found in the Bacillus cereus group, tandem LysM domains in Thermoanaerobacter tengcongensis MB4, etc. in which one of which is found in most examples of endospore-forming bacteria. [Cellular processes, Sporulation and germination]
pfam01476	LysM	6.22e-12	1847	1890	1	42	LysM domain. The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QHW31794.1	1.20e-208	60	1483	37	1546
QJC50841.1	6.19e-196	69	1354	57	1420
QGG54903.1	2.73e-195	69	1329	60	1402
ASS68430.2	1.50e-193	62	1348	52	1418
AYQ73430.1	6.29e-178	61	1100	47	1130

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4QP0_A	2.11e-18	74	348	4	300	CrystalStructure Analysis of the Endo-1,4-beta-mannanase from Rhizomucor miehei [Rhizomucor miehei]
1UUQ_A	8.80e-18	72	292	22	254	Exo-mannosidasefrom Cellvibrio mixtus [Cellvibrio mixtus],1UZ4_A Common inhibition of beta-glucosidase and beta-mannosidase by isofagomine lactam reflects different conformational intineraries for glucoside and mannoside hydrolysis [Cellvibrio mixtus],7ODJ_AAA Chain AAA, Man5A [Cellvibrio mixtus]
3PZ9_A	1.22e-17	153	292	96	223	Nativestructure of endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3PZG_A I222 crystal form of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 [Thermotoga petrophila RKU-1],3PZI_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 in complex with beta-D-glucose [Thermotoga petrophila RKU-1],3PZM_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 with three glycerol molecules [Thermotoga petrophila RKU-1],3PZN_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 with citrate and glycerol [Thermotoga petrophila RKU-1],3PZO_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 in complex with three maltose molecules [Thermotoga petrophila RKU-1],3PZQ_A Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 with maltose and glycerol [Thermotoga petrophila RKU-1]
6TN6_A	5.12e-17	153	292	82	209	X-raystructure of the endo-beta-1,4-mannanase from Thermotoga petrophila [Thermotoga petrophila RKU-1]
1RH9_A	6.50e-15	73	289	5	210	ChainA, endo-beta-mannanase [Solanum lycopersicum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O48540	2.20e-20	151	374	100	359	Mannan endo-1,4-beta-mannosidase 1 OS=Solanum lycopersicum OX=4081 GN=MAN1 PE=1 SV=2
Q0JKM9	2.54e-18	151	289	111	242	Mannan endo-1,4-beta-mannosidase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=MAN1 PE=2 SV=2
Q9SG95	2.05e-16	150	292	102	237	Putative mannan endo-1,4-beta-mannosidase 4 OS=Arabidopsis thaliana OX=3702 GN=MAN4 PE=3 SV=1
Q9FUQ6	3.41e-16	151	374	101	361	Mannan endo-1,4-beta-mannosidase 3 OS=Solanum lycopersicum OX=4081 GN=MAN3 PE=3 SV=1
Q7Y223	7.98e-16	151	292	115	250	Mannan endo-1,4-beta-mannosidase 2 OS=Arabidopsis thaliana OX=3702 GN=MAN2 PE=2 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
0.000296	0.998923	0.000251	0.000187	0.000166	0.000144

TMHMM  Annotations     

start	end
7	29