CAZyme Information: MGYG000001911_01232

Basic Information

• Species: Desulfovibrio sp002159665
• Lineage: Bacteria; Desulfobacterota; Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae; Desulfovibrio; Desulfovibrio sp002159665
• CAZyme ID: MGYG000001911_01232
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
756		83447.56	9.0364

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001911	2704250	MAG	Denmark	Europe

• Gene Location: Start: 19351; End: 21621 Strand: -

Full Sequence      

MLFFLVEIVVALLALAFLVYAILETRSVKKGVSAAKCAVFFQNMDAVAQNVDRDTLPSVS
VLLPVCNEKLVIRKLLLAVCALDYPRDRLEILVLDDSTDETYALVEGMLPRFLEEGVNIR
HLRRESRTGYKAGNLTFGLSKAKGEFIAIFDADCLPPSDFLLRAMPCFGDEKVGFLQTGI
RYVNDNTSFLTRFQAMEAGHKESVTSGLSIEGLMASLTGSSCVWRRACIDAIGGISSATI
TEDVDMGYKAQLMSWKYVWLGNITSRAEFPETMAAFRVQRQRWARGLIQNALRHVREMFQ
TSMPVLSRLYAISLMFSSLLLASFYLVLLLCLPVVFLTPSFGPMFHLVCAIFLAAACVWA
WANTKNSAKTENTTVGKTIGMTLGYVFMHFPISLYYFTAALQVLLRRESGFHRTPKGAGR
KRLSSPRINKILVRLEVFSLCYACLAFIVSINHGLYWVSFYTFLCLVGFSMSLFFSFSDS
RKVCVPSRVVLTGATGSLGSALALEYAAPGRHLILTGRRADVLAKVAQTCRDRGAMVEEH
VLDLENTDAVRNWMRSVCEQNIPDLVIANAGRNTDIGPNLEGEDFGEARALVQVNLLSGM
ALFDATLPFFRKQGGGQFAFTSSLAGYYGLAMTPTYCATKAALKSYGTSLRAWLLKENIH
VNVIFPGYVRSPMCEAMPGPKPFLMEANKAARRIRKGLERDFARISFPFPLNLGVWGLGL
LPLCLAMPIAKILGYGPIQYGQTEKSGPSAQASGQA

Enzyme Prediction     

No EC number prediction in MGYG000001911_01232.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	57	286	2.2e-28	0.9956521739130435

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06437	CESA_CaSu_A2	3.16e-98	57	287	1	232	Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex. Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.
cd06421	CESA_CelA_like	2.29e-54	57	289	1	232	CESA_CelA_like are involved in the elongation of the glucan chain of cellulose. Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.
cd05350	SDR_c6	3.62e-47	489	722	1	232	classical (c) SDR, subgroup 6. These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.
COG1215	BcsA	9.77e-44	1	396	15	403	Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility].
cd06423	CESA_like	5.10e-41	61	243	1	180	CESA_like is the cellulose synthase superfamily. The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SFV72799.1	0.0	1	735	1	729
SPD36508.1	2.01e-303	1	736	1	738
ATD80944.1	2.98e-303	1	736	12	749
ANY15051.1	3.57e-131	4	482	8	487
BAX59879.1	6.19e-129	7	486	10	491

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7LBY_A	5.88e-21	52	289	268	503	ChainA, Cellulose synthase catalytic subunit [UDP-forming] [Escherichia coli K-12]
5EJ1_A	5.36e-19	38	292	101	380	ChainA, Putative cellulose synthase [Cereibacter sphaeroides 2.4.1]
4HG6_A	5.91e-19	38	292	113	392	ChainA, Cellulose Synthase Subunit A [Cereibacter sphaeroides]
4P00_A	5.92e-19	38	292	114	393	ChainA, Cellulose Synthase A subunit [Cereibacter sphaeroides 2.4.1],4P02_A Chain A, Cellulose Synthase subunit A [Cereibacter sphaeroides 2.4.1],5EIY_A Chain A, Putative cellulose synthase [Cereibacter sphaeroides 2.4.1],5EJZ_A Chain A, Putative cellulose synthase [Cereibacter sphaeroides 2.4.1]
3AI1_A	4.88e-16	490	672	11	193	Thecrystal structure of L-sorbose reductase from Gluconobacter frateurii complexed with NADPH and L-sorbose reveals the structure bases of its catalytic mechanism and high substrate selectivity [Gluconobacter frateurii],3AI1_B The crystal structure of L-sorbose reductase from Gluconobacter frateurii complexed with NADPH and L-sorbose reveals the structure bases of its catalytic mechanism and high substrate selectivity [Gluconobacter frateurii],3AI2_A The crystal structure of L-sorbose reductase from Gluconobacter frateurii complexed with NADPH [Gluconobacter frateurii],3AI2_B The crystal structure of L-sorbose reductase from Gluconobacter frateurii complexed with NADPH [Gluconobacter frateurii],3AI2_C The crystal structure of L-sorbose reductase from Gluconobacter frateurii complexed with NADPH [Gluconobacter frateurii],3AI2_D The crystal structure of L-sorbose reductase from Gluconobacter frateurii complexed with NADPH [Gluconobacter frateurii],3AI2_E The crystal structure of L-sorbose reductase from Gluconobacter frateurii complexed with NADPH [Gluconobacter frateurii],3AI2_F The crystal structure of L-sorbose reductase from Gluconobacter frateurii complexed with NADPH [Gluconobacter frateurii],3AI2_G The crystal structure of L-sorbose reductase from Gluconobacter frateurii complexed with NADPH [Gluconobacter frateurii],3AI2_H The crystal structure of L-sorbose reductase from Gluconobacter frateurii complexed with NADPH [Gluconobacter frateurii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q6YWK8	1.97e-39	57	286	118	353	Probable glucomannan 4-beta-mannosyltransferase 11 OS=Oryza sativa subsp. japonica OX=39947 GN=CSLA11 PE=2 SV=1
Q9FNI7	2.49e-38	57	286	97	332	Glucomannan 4-beta-mannosyltransferase 2 OS=Arabidopsis thaliana OX=3702 GN=CSLA2 PE=1 SV=1
Q6Z2T9	4.17e-38	53	286	137	376	Probable glucomannan 4-beta-mannosyltransferase 6 OS=Oryza sativa subsp. japonica OX=39947 GN=CSLA6 PE=2 SV=2
Q6UDF0	1.84e-37	43	312	76	353	Glucomannan 4-beta-mannosyltransferase 1 OS=Cyamopsis tetragonoloba OX=3832 GN=ManS PE=1 SV=1
Q9SRT3	2.12e-37	47	289	211	459	Probable xyloglucan glycosyltransferase 6 OS=Arabidopsis thaliana OX=3702 GN=CSLC6 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.999793	0.000207	0.000004	0.000001	0.000001	0.000022

TMHMM  Annotations     

start	end
4	23
306	328
343	362
383	405
455	477
489	508
713	735