CAZyme Information: MGYG000004823_00561

Basic Information

• Species: CAG-462 sp900765575
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; CAG-462; CAG-462 sp900765575
• CAZyme ID: MGYG000004823_00561
• CAZy Family: GH127
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1047	MGYG000004823_22|CGC1	118666.67	6.5391

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004823	3872922	MAG	China	Asia

• Gene Location: Start: 8970; End: 12113 Strand: +

Full Sequence      

MNIKKVYIAFLFSFSVLALFSQTKEQIKEVPFTKVRLTDCFWAPRMETNRTVSIPSAFKE
CEKNGRFDNFALAGGLIKGEHKGDFSFDDTDPYKVIEGASYSLAVKYDAALDAYLDSVIT
IIAAAQEPDGYLCTCVTNRCERLSGWWGHSRWEKINSHELYNCGHLYEAAVAHFQATGKR
TLLNVAIKNADLICTVFGPEEGKKHVPSGHPIVEMALAKLYKVTGKQEYLALAKYFVEET
GRGTDGHILSAYSQDHQPILQQEEIVGHAVRAGYLYSGVADVAALTQDMAYFHALCRIWE
NMAGKKLYITGGIGSRAQGEGFGPNYELNNHTSYCETCAAIANVYWNHRMFLATGEAKYA
DVAERALYNGVISGVSLSGDKFFYDNPLESMGQHGRQKWFGCACCPGNITRFMASIPYYI
YATQKNSVYVNMYAQGEATIELENNEIRMEQTTAYPYEGRITLKVTPKKKNKWTLRLRIP
GWAQSSPVPSDLYRYTDAPKPYKLYLNGEEVKGDFVDGYAVFERKWKAGDEVTLVLPMEV
RRVSARQEVVDDRGKLAMERGPIVYCLEGKDQADGTVFNKYIPAGTRMEAKMDTSLLGGV
MVLTGVCKEVAHDGSEKEVPFKAVPYATWNNRGAGQMAVWIPEEAAYTHPTPLPTIASRA
RTLSIKAPIQKDAPESASVEEWAWGVNDQWEPKCSADNSKPYYYWWLKQGTLETLAYEFD
RPEHVSGVEVYWLDFDHYDGNYRVPESWKLYYKEGNAWKEVETLDEYGIKKDCYNVLHFK
PVMTSALKIEAQLRKGASGGIIEWKVNGEPYRCTERPVAMPKGMKQPSFYKKYLNQEGFP
IVASANVRDEALMKAYEYMHLMLLKLPAAREAMIQRGCKVIVIGEKEQVSDIPEYAFFTR
TAEEKKYWNARARGFGGSEGDGWCMSGGEENLLNLPGDRYRGENIFIHEFAHLIHGVGLR
STVSGFDDRLQRLYDSAKTKGLWVNTYAMANKEEYFAECVQSYFNCNRYAEKADGVHNSV
NTREKLRHYDPEMYALLSELFYPFFDE

Enzyme Prediction     

No EC number prediction in MGYG000004823_00561.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH127	35	566	2.9e-207	0.9980916030534351

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam07944	Glyco_hydro_127	3.12e-177	35	566	2	503	Beta-L-arabinofuranosidase, GH127. One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context.
COG3533	COG3533	4.56e-171	24	644	6	588	Uncharacterized conserved protein, DUF1680 family [Function unknown].
cd20170	Peptidase_M90-like	2.02e-04	944	1041	117	209	uncharacterized M90 peptidase family-like proteins. This subfamily contains uncharacterized M90 peptidase-like domains, similar to the Mlc Titration Factor A (MtfA) peptidase from Escherichia coli, also known as the YeeI gene product, which is involved in the control of the glucose-phosphotransferase sensory and regulatory system by inactivation of the repressor Mlc (making large colonies). E. coli MtfA has been shown to have aminopeptidase activity with the presence of a single zinc ion in the active site ligated by two histidines in an HEXXH motif. MtfA is related to the catalytic domain of the anthrax lethal factor and the Mop protein involved in the virulence of Vibrio cholerae; although sequence similarity is low, conservation is observed in the overall structure as well as in the residues around the active site.
cd20493	M34_ATLF_C-like	2.89e-04	944	998	121	178	C-terminal catalytically active domain of anthrax toxin lethal factor and similar domains; belongs to peptidase family M34. This subfamily includes the C-terminal catalytic domain of anthrax toxin lethal factor (ATLF; EC 3.4.24.83). ATLF and edema factor are enzyme components of anthrax toxin and are carried into the cell by a third component, the protective antigen (PA). ATLF is secreted by Bacillus anthracis to promote disease virulence through disruption of host signaling pathways. ATLF belongs to peptidase family M34 and has the hallmark metalloprotease motif HEXXH motif where the two His residues bind a single zinc atom, and the Glu has a catalytic role. ATLF is a highly selective protease whose major substrates are mitogen-activated protein kinase kinases (MKKs). MKKs are cleaved by ATLF near their N-termini, removing the docking sequence for the downstream cognate mitogen-activated protein kinase. Preferred amino acids around the cleavage site can be denoted BBBBxHxH, in which B denotes Arg or Lys, H denotes a hydrophobic amino acid, and x is any amino acid. At its N-terminus, ATLF has a related PABD domain which lacks the hallmark metalloprotease motif HEXXH. This subfamily also includes Bacillus thuringiensis Vip2Ac-like_2 which belongs to the Vip family of proteins that are secreted during the vegetative growth phase.
cd20184	M34_peptidase_like	0.001	947	1040	56	131	uncharacterized subfamily of peptidase family M34. Peptidase family M34 (also known as the anthrax lethal factor family) includes the C-terminal catalytic domain of anthrax lethal factor (ATLF, EC 3.4.24.83), and the N-terminal protective antigen-binding domains (PABDs) of ATLF and edema factor (EF). ATLF and EF are enzyme components of anthrax toxin and are carried into the cell by a third component, the protective antigen (PA). ATLF is a highly selective protease whose major substrates are mitogen-activated protein kinase kinases (MKKs). At its N-terminus, ATLF has a PABD domain which lacks the hallmark metalloprotease motif HEXXH, and, at its C-terminus, the related catalytic domain has the HEXXH motif where the two His residues bind a single zinc atom, and the Glu has a catalytic role. EF acts as a Ca2+- and calmodulin-dependent adenylyl cyclase that can cause edema when associated with PA; it is comprised of the PABD and an adenylyl cyclase domain. Pro-Pro endopeptidase (PPEP-1; EC 3.4.24.89, also known as Zmp1) is an extracellular metalloprotease that shows a unique specificity for hydrolyzing a Pro-Pro bond and is involved in bacterial adhesion. This uncharacterized subfamily includes proteins which have an N-terminal SLH domain, and proteins which may have an N-terminal IG-like domain; these proteins have the hallmark metalloprotease motif HEXXH motif.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDO71484.1	0.0	27	807	31	811
QUT89696.1	0.0	22	807	35	820
ALJ59245.1	0.0	22	807	35	820
QQY38942.1	0.0	20	807	24	811
ABR38820.1	0.0	20	807	24	811

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6EX6_A	9.53e-201	27	652	7	634	TheGH127, Beta-arabinofuranosidase, BT3674 [Bacteroides thetaiotaomicron VPI-5482],6EX6_B The GH127, Beta-arabinofuranosidase, BT3674 [Bacteroides thetaiotaomicron VPI-5482]
4QJY_A	4.81e-147	33	644	14	648	Crystalstructure of native Ara127N, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QJY_B Crystal structure of native Ara127N, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus]
4QK0_A	1.66e-143	33	644	14	648	Crystalstructure of Ara127N-Se, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QK0_B Crystal structure of Ara127N-Se, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QK0_C Crystal structure of Ara127N-Se, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus],4QK0_D Crystal structure of Ara127N-Se, a GH127 beta-L-arabinofuranosidase from Geobacillus Stearothermophilus T6 [Geobacillus stearothermophilus]
5MQO_A	1.82e-99	35	642	44	695	Glycosidehydrolase BT_1003 [Bacteroides thetaiotaomicron]
3WRE_A	6.58e-98	69	640	56	655	Thecrystal structure of native HypBA1 from Bifidobacterium longum JCM 1217 [Bifidobacterium longum subsp. longum JCM 1217],3WRG_A The complex structure of HypBA1 with L-arabinose [Bifidobacterium longum subsp. longum JCM 1217]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
E8MGH8	3.60e-97	69	640	56	655	Non-reducing end beta-L-arabinofuranosidase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=hypBA1 PE=1 SV=1

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
0.024649	0.928501	0.045976	0.000294	0.000264	0.000270

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004823_00561.