CAZyme Information: CDH49868.1

Basic Information

• Species: Lichtheimia corymbifera
• Lineage: Mucoromycota; Mucoromycetes; ; Lichtheimiaceae; Lichtheimia; Lichtheimia corymbifera
• CAZyme ID: CDH49868.1
• CAZy Family: CE4
• CAZyme Description: related to glycerol-3-phosphate-acyltransferase-laccaria bicolor

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1527		172331.91	7.6142

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_LcorymbiferaJMRCFSU9682	12379	1263082	97	12282

• Gene Location: location=CBTN010000004:527059-532466(-)

Full Sequence      

MQSKDEIRQRIQQLTGAIEKHRKDQTNNHARGGYSGAHYSNRPMSFSRTWTNNHNRGSPN
KSAIFNGPRNAPATSHSYNKRLVLNKTEASTRPPQPRIPPSSSSSPHKKLVLNNTTAKPP
KPTFSATTTTTTAPGAPKQIEIGGVKFMVKGKKLIRQDRLKNQPLPSGMAAGSHVVVVRR
NKRTRPPGSDPGAAKKMRPTTARSRKGNMVFVRGPEGYVRQGASGKSLVLKSKRVTRRYC
GHYTRYGKCPQQPRCPFIHDPKRRAICPRFLQNKCPKPANLCRLSHQPTPNIIPHCVHFQ
RGRCTNTDCIFSHVHVRPDAPVCRAFAMEGYCSKGLECREKHIHVCPEFAETGKCSNANC
RLPHVARRAATGGQGTAGIIRPGTWVSTAYWHEQRKLQADSNNKRTANRTLSNIPPPSNS
NSSDSNNMTTPRPTREEEEQQGFVRLFDDSEEDEGWSQYLSQDHVQEESSQLHFSDNDED
EEDENSSEGDSDSNMDEDEDEEVDEEDEEVDEYEIAEDDGEYIEEEQVIAKPPVNPQYSF
FTFLYSIYLFWMFIDALLVCVIFLTGWIVCDDTTSAPVNHLVAFGDSYTADKGDECNGPK
WIRQLAWDNITIDNHAVGGAYCVDTNNTRSPSVNQQTMHYINSMPDDDPATTIYVIFVGI
NDMVGHVQPTDVLRCISNQIDRLHQTVDANRFLVFNMVPFDKSPREAAEQAMAQAWIEQF
NEQLNTTITEKSAQYKDMHMVLIDTHTIISQVLDNPESYGITQGTTDYYARTHNPRQDND
KLDNGNVYFWFDKAHMTNVVHAQLSKSIVEQNPFPSMNLMSTGGSSTSYKISPVYFCAHG
RCDKTTIDWPISFCFPAHTTTHASPPVGGVVSFLLLATHSPAMPFGLGHEFVILVSRSAL
WSFFVDIKLQDEHNIPTEGPMIVAATHHNMIVDPAVLSVTFPDHRRFHYWAKDSIFKHPL
AKRFLENCGVVPVDRKTRNNAQLYAATYDVMRLGESVAVFPEGTSHTLPHLGTFKDGTSF
AALEYAKVIEEDPHPNADGSLPRKAVILPVGIVYPEKSKYRSVAIVKYGKPLHVDPYMDT
YYQDPKKAAKQLTTDLRSAIEGLTVNAPDWESRDAAEMARWLLFPGENGSMRDYISVTQS
LIGAFADLSSSDPDIALLEQSLRAYKMELEALSLKDSHIAKYNERDITAASTTVELLRRT
MASMIDLPLFLPGLVGHLPLYLAGYYAGKFEIYEEVRAQNKIFLGLLMVPFVYILAFIWG
WYTLFGGTFFGFFAALATLGVFVWYHVVSIDERYENFKDLVGRWRLFDAVVLGRGMWRRK
DRILQLKQLRDSNLQGVRRMVKAYKGKNDHVHAVWLAIRSRVKQFGDPAKLHGRRKKLAK
QFEWSFEDHGNPFGSIYKSFLGDPALSNTMLKTLYSWIFPPPLTPEELAQVEQQVEDLIK
NNNVVVFSKTYCPFCSSAKELLKSQNVEFTVVELDREAHGSAMQDYLEKRSGQRTVPNIF
IKQQHIGGCDDLKAADRDGRLQKMLAA

Enzyme Prediction     

No EC number prediction in CDH49868.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE16	593	807	2.7e-23	0.8651685393258427

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
153254	LPLAT_AAK14816-like	8.51e-51	894	1101	3	203	Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown AAK14816-like. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are uncharacterized glycerol-3-phosphate acyltransferases such as the Plasmodium falciparum locus AAK14816 putative acyltransferase, and similar proteins.
239511	GRX_GRXh_1_2_like	1.29e-40	1444	1524	2	82	Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, which are members of this subfamily. Also included in this subfamily are the N-terminal GRX domains of proteins similar to human thioredoxin reductase 1 and 3.
274016	GRX_euk	1.12e-35	1444	1525	1	83	Glutaredoxin. Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This model represents eukaryotic glutaredoxins and includes sequences from fungi, plants and metazoans as well as viruses.
238882	fatty_acyltransferase_like	2.51e-33	580	811	1	270	Fatty acyltransferase-like subfamily of the SGNH hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases. Might catalyze fatty acid transfer between phosphatidylcholine and sterols.
223282	PlsC	2.43e-28	870	1120	11	249	1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDS11360.1|CE0	9.80e-24	574	835	40	319
CDS06616.1|CE0	2.56e-22	575	809	28	278
CDS09080.1|GT22	2.58e-13	1435	1525	500	590
UJR13476.1|CE0	3.05e-10	573	829	24	295
UQO47878.1|CE16	1.63e-09	565	821	168	451

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KQA_A	4.53e-24	1424	1525	19	120	Crystal structure of buckwheat glutaredoxin-glutathione complex [Polygonaceae]
5GTX_A	6.78e-23	1424	1525	16	117	Crystal structure of mutated buckwheat glutaredoxin [Polygonaceae],5GTX_B Crystal structure of mutated buckwheat glutaredoxin [Polygonaceae]
2LV3_A	5.89e-22	1426	1525	16	115	Structure-functional characterization of Grx domain of Mus musculus TGR [Mus musculus]
5ZVL_A	9.04e-21	1434	1525	55	146	Crystal Structure of Wheat Glutarredoxin [Triticum aestivum],5ZVL_B Crystal Structure of Wheat Glutarredoxin [Triticum aestivum],5ZVL_C Crystal Structure of Wheat Glutarredoxin [Triticum aestivum],5ZVL_D Crystal Structure of Wheat Glutarredoxin [Triticum aestivum],5ZVL_E Crystal Structure of Wheat Glutarredoxin [Triticum aestivum]
3H8Q_A	5.54e-20	1430	1525	5	100	Crystal structure of glutaredoxin domain of human thioredoxin reductase 3 [Homo sapiens],3H8Q_B Crystal structure of glutaredoxin domain of human thioredoxin reductase 3 [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|B7ZFT1|GLRX1_RHIID	1.65e-30	1428	1527	1	100	Glutaredoxin-1 OS=Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194) OX=747089 GN=GRX1 PE=2 SV=3
sp|O74823|YBJC_SCHPO	1.82e-30	224	382	184	355	Zinc finger CCCH domain-containing protein C337.12 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPBC337.12 PE=4 SV=3
sp|O81187|GLRX_VERFO	5.45e-24	1434	1525	5	96	Glutaredoxin OS=Vernicia fordii OX=73154 PE=3 SV=1
sp|P55143|GLRX_RICCO	3.31e-23	1434	1525	5	96	Glutaredoxin OS=Ricinus communis OX=3988 PE=3 SV=1
sp|Q9ZR41|GLRX_SOLLC	5.41e-23	1434	1525	5	96	Glutaredoxin OS=Solanum lycopersicum OX=4081 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000054	0.000000

TMHMM  Annotations     

Start	End
547	569
1207	1229
1242	1264
1269	1288