CAZyme Information: MGYG000001542_03350

Basic Information

• Species: Paenibacillus_A sp900069005
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A sp900069005
• CAZyme ID: MGYG000001542_03350
• CAZy Family: GH8
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1763		194445.57	4.6574

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001542	5846629	Isolate	not provided	not provided

• Gene Location: Start: 30698; End: 35989 Strand: +

Full Sequence      

MKNLVKPKWRRHPSLLLIFMLLFQLAGVVSADGPPVDHAKGVAPEYLANNMEEWIGEDAA
APILESVQNATTDAVYVAQSLDQEVIAQWVFQNGGDNGTFVATGGQYQSASILTNVGGVF
ENYSGSKQEISYQGWDQGNGKKYWLVTMSTAGFENIAISSEQNSSGSGPNDFKLQMSTDQ
ATWTDVKNGIIQMNTSSSYNCPQDTCKLKNLPLDGADDKELLYIRWVVNSNTPTNTVDNP
SGIGGGGSSRIRNIYVTGDPIAGKTPVIPTMDLSQLPKHGAEKVAVDAPLTVKFNKNISI
SKPSVSIIDGNGHEIEATAAVSGGHTLRINHPEFMYGATYTVSIPRQAIMAEDGVPLVRD
ISWSFTTQDSPLIPKLINMTFNAKPKTGIAFAWYTDIMTATKVQVVEASRMTGGAFPEQE
AMEFTGTGEEIGTFMSKADRSTGYKAKFISHKAAANNLKPGTRYRFRVGNGQEWSKVGSF
TTDTAQHQPYRFIVGSDSQASSKEDFEPWADTFKKARDYIGDPKFLINAGDLVDNGDLEE
QWQWMLGVAQDELLNVPFVPVLGGHEIQDYDGDETTPNNNFYNHFNLPRKVVAATHDGSV
YAFEYGDALYMVYNSQFDGKLNEDGTVNWDDDQHEQFWNQVDWMRNTVAKSDKKWKFVTF
HKSPYAAGDNSAQWEGERIEFYKKNLIPVFDELGIDMVFEAHDHMYMRSFQMYGDQIIDP
TSLDKDGEGNVINPQGTVYLMSNAFGNKFYYKNYQYELDENWEPQLIYDENGDPIWYDDY
FAAVDEQPEKKMFTDVSISDQVMKFTAYTAAVEDEGKAEAVGNGLIDYDHYGIKRTDSKP
NPVEAAKVTLKGSKAVLTWTVPKNSKEPVRGFRIYEKNDKIKTYWSKYITVKDGQTEYSY
TVEGINPEKNYDFMIKSVGRRDNSAPVEISTLGGPVNQEPPSEPGNLKGTGASAFQINLT
WEASPGTVSPSGYHIYRDGSLAGTTEATSYNDIGLKPDTSYRYVVKAFNAEGIESLGSNE
IVVKTKQAPAGEGPHKAFPQHTSYVQGSIKPNHVTQSQMDQTVGRLYDEWKAKYLKKHPY
LQKTDPAQYYVWYADGDWFEEEYDEELGVDYMATTVSEAHGYGMLITALMGGHDPDAKQY
FDGLFRYFKAHPSEINPNLMAWKQGDTGTAIVDVDGVDSATDGDMDIAYALLLADSQWGS
SGEINYLAEAKRMINAIMDNEVNQSDWMLRIADWATSGKWAAATRPSDFMLQHMKDYRNV
TGDSKWDRVVDTTYGMIHELYSGYSPNAGLLPDFVLKSGGKFVPAEPNFLESDYDGDYSY
NSSRTPWRIGTDYLVTGDVRAKDQLSTLNRWIRGMTNGDPDQILAGYKLDGSQALEEYGD
ITFSAPLMVSAMIDSSNQEWLNKLWDHNAAVRTEDDVYFGNNLRLLSMIVVSGNWWTPTI
VDTEAPAEPTIDRAEAVSGTAVDLKWTPSGDNLGVAGYKVYRNDQVISTTTKTEYRDTGL
SAGTTYKYFVVAFDAAGNLSKMSNIRYVTTLQSPGGGSPGDSTGGSSDGGANSPPKTTDP
GAGTDLTSEPDKQPETSTPAKKSFRDVGEKYAWAKNAIEELAGAGIIKGKTESTFEPGKR
ISRADFIVLLVRALGLKADFDANFADVASGAYYSEALGIAKQLGIAVGIGGNKFEPMAHI
SRQDMMVLTARALKLAGKMNEAGSAVDLGKFTDSSKLAEYAVESVASLAKAGIILGDGRA
IHPAQSATRAEVAVMIHRFYTRP

Enzyme Prediction     

EC	3.2.1.132	3.2.1.73	3.2.1.4

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH8	1106	1430	3.1e-73	0.928125

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam01270	Glyco_hydro_8	4.84e-21	1115	1429	32	317	Glycosyl hydrolases family 8.
cd00839	MPP_PAPs	1.79e-17	486	776	1	255	purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain. Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.
COG3405	BcsZ	2.27e-11	1115	1438	53	353	Endo-1,4-beta-D-glucanase Y [Carbohydrate transport and metabolism].
pfam16656	Pur_ac_phosph_N	2.32e-11	374	482	1	94	Purple acid Phosphatase, N-terminal domain. This domain is found at the N-terminus of Purple acid phosphatase proteins.
pfam00149	Metallophos	4.19e-10	490	706	1	191	Calcineurin-like phosphoesterase. This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AZS18334.1	0.0	25	1762	1	1736
AJS61487.1	0.0	85	1758	27	1703
AIQ25865.1	0.0	73	1762	15	1696
QNN60665.1	0.0	243	1533	14	1281
QTH45936.1	9.40e-235	366	1027	747	1383

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5XD0_A	9.12e-135	1034	1437	33	408	ApoStructure of Beta-1,3-1,4-glucanase from Paenibacillus sp.X4 [Paenibacillus sp. X4],5XD0_B Apo Structure of Beta-1,3-1,4-glucanase from Paenibacillus sp.X4 [Paenibacillus sp. X4]
7CJU_A	3.84e-87	1036	1444	11	396	Crystalstructure of inactive form of chitosanase crystallized by ammonium sulfate [Bacillus sp. K17-2],7CJU_B Crystal structure of inactive form of chitosanase crystallized by ammonium sulfate [Bacillus sp. K17-2],7XGQ_A Chain A, chitosanase [Bacillus sp. K17-2],7XGQ_B Chain B, chitosanase [Bacillus sp. K17-2]
1V5C_A	1.79e-86	1036	1438	5	384	Thecrystal structure of the inactive form chitosanase from Bacillus sp. K17 at pH3.7 [Bacillus sp. (in: Bacteria)],1V5D_A The crystal structure of the active form chitosanase from Bacillus sp. K17 at pH6.4 [Bacillus sp. (in: Bacteria)],1V5D_B The crystal structure of the active form chitosanase from Bacillus sp. K17 at pH6.4 [Bacillus sp. (in: Bacteria)]
1CEM_A	3.10e-41	1039	1438	4	359	ChainA, CELLULASE CELA (1,4-BETA-D-GLUCAN-GLUCANOHYDROLASE) [Acetivibrio thermocellus],1IS9_A Chain A, endoglucanase A [Acetivibrio thermocellus]
1KWF_A	6.48e-40	1039	1438	4	359	ChainA, Endoglucanase A [Acetivibrio thermocellus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P19254	1.37e-134	1034	1437	33	408	Beta-glucanase OS=Niallia circulans OX=1397 GN=bgc PE=3 SV=1
P29019	1.35e-84	1018	1438	43	440	Endoglucanase OS=Bacillus sp. (strain KSM-330) OX=72575 PE=1 SV=1
A3DC29	4.61e-39	1029	1449	26	402	Endoglucanase A OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celA PE=1 SV=1
C6CRV0	9.30e-37	1583	1760	1282	1459	Endo-1,4-beta-xylanase A OS=Paenibacillus sp. (strain JDR-2) OX=324057 GN=xynA1 PE=1 SV=1
P37699	3.51e-31	1038	1435	38	389	Endoglucanase C OS=Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) OX=394503 GN=celCCC PE=1 SV=2

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
0.000254	0.999123	0.000165	0.000164	0.000146	0.000136

TMHMM  Annotations     

start	end
13	31