CAZyme Information: MGYG000004435_00421

Basic Information

• Species: UBA7597 sp900767195
• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; Borkfalkiaceae; UBA7597; UBA7597 sp900767195
• CAZyme ID: MGYG000004435_00421
• CAZy Family: GH109
• CAZyme Description: Alpha-N-acetylgalactosaminidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
432		48984.8	5.0361

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004435	1980556	MAG	Israel	Asia

• Gene Location: Start: 36176; End: 37474 Strand: -

Full Sequence      

MKKVKVGVIGLGQRGMSLLWAMMACEEAEIVAVCDVYEDRREAGAKRVKETRGNDVKQYE
DYRELIDDKNVEAVVITSSWDEHTRMAVYSMKAGKYTAVEVAGAYDIEDCWQLVRTYEET
RTPIMMLENCCFDKFELLSTSLVRSGKLGKIVYCHGAYAHELRGEVLGGNVNRHYRLKNY
ELRNCENYPTHELGPIAKILNINRGNKMLSLTSVATKSWGLTECAKSDRSPDPSLKDTEF
NQGDIVVTTITCAGGEVITLRLDTSLPRCYSREFTVRGTKGLCEQDTNMVLLETDKFLHD
DFEAIKTVEKHMNCAEEYSHYLPEVWHDMTEEEKKLGHGGMDYLEFKAFFTAILNGTEMP
IDVYDMAAWMAITPLSEQSIAHGGMPQAIPDFTRGKWMYRPVLDVTELPEVREEDAAGEG
KEMKNALGYSRK

Enzyme Prediction     

No EC number prediction in MGYG000004435_00421.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH109	1	398	6.9e-137	0.9874686716791979

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0673	MviM	4.66e-20	1	160	1	157	Predicted dehydrogenase [General function prediction only].
pfam01408	GFO_IDH_MocA	9.57e-11	4	120	1	112	Oxidoreductase family, NAD-binding Rossmann fold. This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.
PRK08618	PRK08618	2.95e-05	2	105	125	223	ornithine cyclodeaminase family protein.
PRK10206	PRK10206	0.001	61	152	55	146	putative oxidoreductase; Provisional
cd05284	arabinose_DH_like	0.005	6	108	174	274	D-arabinose dehydrogenase. This group contains arabinose dehydrogenase (AraDH) and related alcohol dehydrogenases. AraDH is a member of the medium chain dehydrogenase/reductase family and catalyzes the NAD(P)-dependent oxidation of D-arabinose and other pentoses, the initial step in the metabolism of d-arabinose into 2-oxoglutarate. Like the alcohol dehydrogenases, AraDH binds a zinc in the catalytic cleft as well as a distal structural zinc. AraDH forms homotetramers as a dimer of dimers. AraDH replaces a conserved catalytic His with replace with Arg, compared to the canonical ADH site. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALS29040.1	2.42e-139	4	400	5	398
QTH43530.1	3.94e-137	3	400	4	398
QUO31207.1	1.01e-134	1	400	1	398
QTH41319.1	2.93e-133	3	398	7	398
AVM42018.1	8.04e-133	1	399	1	398

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2IXA_A	1.68e-80	2	397	19	431	A-zyme,N-acetylgalactosaminidase [Elizabethkingia meningoseptica],2IXB_A Crystal structure of N-ACETYLGALACTOSAMINIDASE in complex with GalNAC [Elizabethkingia meningoseptica]
6T2B_A	2.37e-63	3	408	42	449	Glycosidehydrolase family 109 from Akkermansia muciniphila in complex with GalNAc and NAD+. [Akkermansia muciniphila],6T2B_B Glycoside hydrolase family 109 from Akkermansia muciniphila in complex with GalNAc and NAD+. [Akkermansia muciniphila],6T2B_C Glycoside hydrolase family 109 from Akkermansia muciniphila in complex with GalNAc and NAD+. [Akkermansia muciniphila],6T2B_D Glycoside hydrolase family 109 from Akkermansia muciniphila in complex with GalNAc and NAD+. [Akkermansia muciniphila]
3EC7_A	1.17e-13	4	158	24	176	CrystalStructure of Putative Dehydrogenase from Salmonella typhimurium LT2 [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],3EC7_B Crystal Structure of Putative Dehydrogenase from Salmonella typhimurium LT2 [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],3EC7_C Crystal Structure of Putative Dehydrogenase from Salmonella typhimurium LT2 [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],3EC7_D Crystal Structure of Putative Dehydrogenase from Salmonella typhimurium LT2 [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],3EC7_E Crystal Structure of Putative Dehydrogenase from Salmonella typhimurium LT2 [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],3EC7_F Crystal Structure of Putative Dehydrogenase from Salmonella typhimurium LT2 [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],3EC7_G Crystal Structure of Putative Dehydrogenase from Salmonella typhimurium LT2 [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2],3EC7_H Crystal Structure of Putative Dehydrogenase from Salmonella typhimurium LT2 [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]
3EZY_A	6.60e-10	4	150	3	144	Crystalstructure of probable dehydrogenase TM_0414 from Thermotoga maritima [Thermotoga maritima],3EZY_B Crystal structure of probable dehydrogenase TM_0414 from Thermotoga maritima [Thermotoga maritima],3EZY_C Crystal structure of probable dehydrogenase TM_0414 from Thermotoga maritima [Thermotoga maritima],3EZY_D Crystal structure of probable dehydrogenase TM_0414 from Thermotoga maritima [Thermotoga maritima]
3E18_A	2.24e-09	1	157	3	156	CRYSTALSTRUCTURE OF NAD-BINDING PROTEIN FROM Listeria innocua [Listeria innocua],3E18_B CRYSTAL STRUCTURE OF NAD-BINDING PROTEIN FROM Listeria innocua [Listeria innocua]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A4Q8F7	9.17e-80	2	397	19	431	Alpha-N-acetylgalactosaminidase OS=Elizabethkingia meningoseptica OX=238 GN=nagA PE=1 SV=1
B2FLK4	5.22e-78	2	400	32	444	Glycosyl hydrolase family 109 protein OS=Stenotrophomonas maltophilia (strain K279a) OX=522373 GN=Smlt4431 PE=3 SV=1
A4Q8G1	2.32e-76	4	400	53	462	Alpha-N-acetylgalactosaminidase OS=Tannerella forsythia OX=28112 GN=nagA PE=3 SV=1
A6KY05	5.37e-73	4	400	17	413	Glycosyl hydrolase family 109 protein 2 OS=Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC 11154) OX=435590 GN=BVU_0611 PE=3 SV=1
Q01S58	2.94e-72	4	400	43	435	Glycosyl hydrolase family 109 protein OS=Solibacter usitatus (strain Ellin6076) OX=234267 GN=Acid_6590 PE=3 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
1.000062	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004435_00421.