CAZyme Information: MGYG000003402_00311

Basic Information

• Species: Paenibacillus lactis
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus lactis
• CAZyme ID: MGYG000003402_00311
• CAZy Family: GH163
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1068		119448.36	4.5977

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003402	5924245	MAG	United States	North America

• Gene Location: Start: 1552; End: 4758 Strand: -

Full Sequence      

MKALNGTSGIKLIVTMFMAVFMMVLAASANAEETGEKEKGRPPHPHSILIKNGVAQADIL
ISPAADDMEMYAAQELQQTLKMVSGATLPIYRADTEQNSVSAYLQQDQLNIQKSGAYPVS
FDFLNNHGRSTVVEVVYSEGNAFPIRLNAPIELQKDQAGSITGTLYVPPSTADGTYQLSF
EARSDGQSIGSMELEVTLNRNTLLNGGFEESVKEGWYSTTAAQDSEVSHSGSSSLRLASN
NVRSNQPFRLERGKQYKLKAWVKGAKNGTARMQVNEMANPYNVKHSVFSSFSVTTDWTEV
ELIYHADEHRPYDYHWLVFSFLQGNGPGTLWIDDVTLAEVEEEGSSEPPGPPPVVDYGPA
HNRIQLVLSTTDRIPSNQDTAYLANSDGFAIRQKGSRIYILGSEARGILNGVYDFLEENA
GVLWTRSKELGTLYDPLPTVTATRTNYAEKSPIPLRGWLTLGMGENGDGGSDQATDVMLA
RNKNNIKMSDSSNRLLWDRFARTGLTPVMLGHNLAFWLPNDEYFAEHPDYYNMKDGKYIP
LSDSTQINFYHPEVPGVIAAKAKKLIASRNIDYIGIGINDNSSFDQGELSRQPFTTEDGV
VVQPEDPAYRSTVFFSFLNKVAREIHADYPDVKIVSYAYTFTDTPPKVDLEDNIVLVYAP
LYEDAREPLNSSNTSNPNYAYNEKLRGWAEKTKNILVYNYYGSFPSDAYERPIAAKVQAD
LQYYRELGILGVLPEGTVDAGNDAWGINALQYWLFNKLFWNPDEDIEALKTQFINKAYGA
AAEPMRRYYDLIEQGWNYDQSQQSWATSGESLVRQYVIVAGIRDQAQQALDEAYALADGK
AKARIEPIKTTFERMVEIAEDSVNISANAVRTTASKDQILNTLDFGAGPWRAVESPVTYF
KDMSSGKLPPVLTKVYLLWDEEYIYIGYENFDPDPSKMVISDTAPNEWWLSGKDDSVETY
LMDGTPGSSSYYAFMTNALPLNLDYKGPEKSPDWTRPWESRAEVKFDRWNVIQAIPFSSI
QFDPDESRTLTGLFFRNYHRSGSGLGLYGWAGGAVWNPADFRPIHLRD

Enzyme Prediction     

No EC number prediction in MGYG000003402_00311.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH163	518	789	1.7e-70	0.9920318725099602

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam16126	DUF4838	2.50e-49	511	789	2	263	Domain of unknown function (DUF4838). This family consists of several uncharacterized proteins found in various Bacteroides and Chloroflexus species. The function of this family is unknown.
cd09618	CBM9_like_2	1.87e-12	906	1042	39	175	DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized subfamily are typically found at the N-terminus of longer proteins that lack additional annotation with domain footprints.
cd09620	CBM9_like_3	8.31e-09	890	1065	10	193	DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily may co-occur with various other domains.
pfam02018	CBM_4_9	0.002	201	304	2	115	Carbohydrate binding domain. This family includes diverse carbohydrate binding domains.
pfam06452	CBM9_1	0.002	892	972	12	82	Carbohydrate family 9 binding domain-like. CBM9_1 is a C-terminal domain on bacterial xylanase proteins, and it is tandemly repeated in a number of family-members. The CBM9 module binds to amorphous and crystalline cellulose and a range of soluble di- and monosaccharides as well as to cello- and xylo- oligomers of different degrees of polymerization. Comparison of the glucose and cellobiose complexes during crystallisation reveals surprising differences in binding of these two substrates by CBM9-2. Cellobiose was found to bind in a distinct orientation from glucose, while still maintaining optimal stacking and electrostatic interactions with the reducing end sugar.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANY71258.1	0.0	1	1068	1	1068
QNK60258.1	0.0	42	1068	418	1446
QTH43592.1	0.0	49	1066	470	1647
QJD84461.1	0.0	49	1066	488	1661
BBH18867.1	0.0	43	1066	445	1634

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

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
0.000258	0.999101	0.000180	0.000157	0.000146	0.000131

TMHMM  Annotations     

start	end
7	29