CAZyme Information: MGYG000003595_00189

Basic Information

• Species: HGM11525 sp900770405
• Lineage: Bacteria; Firmicutes_A; Clostridia; Monoglobales_A; UBA1381; HGM11525; HGM11525 sp900770405
• CAZyme ID: MGYG000003595_00189
• CAZy Family: GH151
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
654	MGYG000003595_25|CGC1	72854.3	5.3955

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003595	2475226	MAG	Fiji	Oceania

• Gene Location: Start: 13656; End: 15620 Strand: -

Full Sequence      

MKFRQVHLDFHTSEKLENIGADFNKEEFCRALRAGHVNSITLFSKCHHGWSYHPTKVNEM
HPHLDFDLLGAQIEAAHEAGVRAVVYISAGLDEKYAVAHRGQVIRKSDESTIWATDFMQP
NYHRLCMNTPYLDFLLAQIKEMLENYDADGLFLDIAAVETCYCESCMNTLIGEGKDPEDL
REVTALAEHVYKNYTRRVREVVDSVRPGLPVFHNGGHIRIGRRDLAYANSHLELESLPTG
GWGYDHFPVTAAYARTLGMEYLGMTGKFHTTWGEFGGFKHPNALRYEVSLAAACGASSSI
GDQMPPNGRLDPATYELIGAAYSELEEKEEYLEGARNISDIGVFGLEAFENSGEDAIVSE
AKVRECDAGCARILLEGKYLFDYIDIDEDFAKYKLIILPDRIRVNARLREKLAEYAARGG
KIMASGISATDGDGSFVVDLGAENICANEFKPSYCRPKFEIPSLGNSAYVVYADAYKLGG
VTGEVAAERENPYFNRTREHFCSHQHAPANPDSAQPAVVIGKNGAYIGWNIFEEYEAVGS
LCVKEIVCGVIDRLLTEKSLVTNLPAQGVATLTEQSGRKIVHLLYASPVRRGKAIEIIED
ILPVYGTHVALRCDSAPKRVYLAPQNVDIAFDWRNGYAHFDVDKFECHQMIAVQ

Enzyme Prediction     

EC	3.2.1.51

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH151	25	155	9.4e-51	0.9847328244274809

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam14871	GHL6	1.63e-27	24	155	1	135	Hypothetical glycosyl hydrolase 6. GHL6 is a family of hypothetical glycoside hydrolases.
cd03143	A4_beta-galactosidase_middle_domain	3.75e-07	372	429	33	90	A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. A4 beta-galactosidase middle domain: a type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to beta-galactosidase from Thermus thermophilus. Beta-Galactosidase hydrolyzes the beta-1,4-D-galactosidic linkage of lactose, as well as those of related chromogens, o-nitrophenyl-beta-D-galactopyranoside (ONP-Gal) and 5-bromo-4-chloro-3-indolyl-beta-D-galactoside (X-gal). This A4 beta-galactosidase middle domain lacks the catalytic triad of typical GATase1 domains. The reactive Cys residue found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow in typical GATase1 domains is not conserved in this group.
pfam08532	Glyco_hydro_42M	0.002	382	429	47	94	Beta-galactosidase trimerisation domain. This is non catalytic domain B of beta-galactosidase enzymes belong to the glycosyl hydrolase 42 family. This domain is related to glutamine amidotransferase enzymes, but the catalytic residues are replaced by non functional amino acids. This domain is involved in trimerisation.
COG1874	GanA	0.004	381	464	446	520	Beta-galactosidase GanA [Carbohydrate transport and metabolism].
cd05269	TMR_SDR_a	0.009	73	187	85	179	triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs. TMR is an atypical NADP-binding protein of the SDR family. It lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Proteins in this subgroup however, are more similar in length to the classical SDRs. TMR was identified as a reducer of triphenylmethane dyes, important environmental pollutants. This subgroup also includes Escherichia coli NADPH-dependent quinine oxidoreductase (QOR2), which catalyzes two-electron reduction of quinone; but is unlikely to play a major role in protecting against quinone cytotoxicity. Atypical SDRs are distinct from classical SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCJ93865.1	2.15e-271	1	654	1	659
BCJ98360.1	5.70e-271	1	654	1	657
QNK60374.1	1.65e-265	1	653	1	654
QHT63046.1	7.25e-261	1	654	1	663
AFH63272.1	1.22e-260	1	654	1	658

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6TVK_AAA	9.69e-239	1	654	30	686	ChainAAA, Alpha-L-fucosidase [Paenibacillus thiaminolyticus]

Swiss-Prot Hits     

has no Swissprot hit.

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
1.000075	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003595_00189.