CAZyme Information: OAG24007.1

Basic Information

• Species: Alternaria alternata
• Lineage: Ascomycota; Dothideomycetes; ; Pleosporaceae; Alternaria; Alternaria alternata
• CAZyme ID: OAG24007.1
• CAZy Family: GH93
• CAZyme Description: Chitin synthase [Source:UniProtKB/TrEMBL;Acc:A0A177DWI4]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1834	KV441472|CGC13	205792.18	7.1490

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AalternataSRC1lrK2f	13577	N/A	111	13466

• Gene Location: location=KV441472:1112837-1120382(-)

Full Sequence      

MMLSAWMARCGINARVVDKRGTKIYSGQADGLQLRSLEIFDSFGFADRAWKEANHLIENP
GKDGVIRRSDGVPDTPPGLSRFKEIVLHQGRIERFFLDHIKKHSKDTLRVERAVLPESLH
IAEDRVDDHSPDNYPITVQLRYLTEDEAKPAQSKGSGINDGLFRSNLADDDTEDLIAKSQ
QKEGSTETVRAKYVPTDHIWGVLDIIPITDFPDVRKRCAIHSESSGSMMIIPRENKLARL
YIQLTEIKPDASGRADRSKITPDTILTAAQKIIAPYKLTYEYCDWWTAYQIGQRVGKNFD
HKSRVFLAGDSVHTHSPKAGQGMNVSMQDGYNLGWKLGLVVKGIAQPSILKTYQSERRRI
AQDLIAFDHKFSRLFSGRPAKDVMDEEGVSMDEFKQAFLKGQLFATGLSVDYGTSMLVGK
PGNAADQGDGTDVSSKFEIIGKQELASETKLGMRFPSYQVINQSDGRAWEFQQKLKSDGR
FRIVVFAGNVANAQQSARLKGFCESLSSSSLLAPHLIKNVEVLTLHSSKRKEVELLRDFP
DILHPFDSKFGWDYDSVYADDANPFEGFGDAYKGYGVDRETGCVVKDRRSTIRSCVGSGG
AQSDASFVLHCQFLFFSSLAYFETRGSPHLSTSMTHPALCILDSRFISLGSSYIIVIDDC
YEVLSVIVIAFIRWMVRPLHPYRIFAHLNHSSGFTKNYDTFHIPISVFAAHTHTMDGSTP
HSGSHYGRPPAYDYDDGSPQQLQGGSTMRLLTNVDDSQSYMQRPSFEDTSNMSSANSNTA
ELGARMTMSEVGKQKAAESDIHDFLREAGDALSSTSSTAAAPTQMPRRKMINSETANYAA
LSTTVRSQDPDLQLRDLRRPPSPVSRTYHPTSSSVSGLSRTPSVMDTAPNMPPPDDDYVP
YRRPLSPDRPYSPTRTSDDYSRPPASVNSYEPLDLHGSPRPGSPQRPLPPAPLFTNGARP
GSRGSENTMDMTDMTSIPIHDDDDPFTDIGDDRPDLRSRDSYMSDDTYTDIYTEIDEKAE
HYGPAPDGAQERRGARDAVMTKKEVRLINGELILECKIPTILHSFLPRRDDIEFTHMRYT
AVTCDPDDYIDRGYKLRQNIGNQRETELFIAITMYNENEIDFTRTMHGVMQNISHFCSRM
KSRTWGKDGWQKIVVCIIADGRGKVHPRTLDAIAAMGCFQEGIAKNHVNQKEVTAHVYEY
TTQVSLDSDLKFKGAEKGIVPCQMIFCLKEKNSKKLNSHRWFFNAFGRALNPNVCILLDV
GTKPGPKALYHLWKAFDTDSSVAGAAGEIKAGKGKAWLGLLNPLVASQNFEYKMSNILDK
PLESVFGYITVLPGALSAYRYHALQNDHTGHGPLSQYFKGETLHGQDADVFTANMYLAED
RILCWELVAKRSEQWVLKYVKAATGETDVPDAVPEFISQRRRWLNGAFFAAVYSLLHFKQ
VWATDHTIGRKILLHIEFVYQFVQLLFTFFSLANFYLTFYFVAGSLSDPELDPFGHNIGK
YIFYILRYTCTLLICMQFILSMGNRPQGAKKMFFWSMVMYGIIMAYTTFASFYIVIVQLK
DPKAPKTIGANVFTNLIVSMGTTVGLYFLMSFMYLDPWHMFTSSAQYFALLPSYIATLQV
YAFCNTHDITWGTKGDNVAKTDLGDAKGKNKDVVELEMPSEQLDIDSGYDEALRNLRDRV
EVPEPPISESQQQEDYYRAVRTYMVVIWLISNAIFAMAISEAYSDRKVTNNFYLTFILWA
VAGLAFFRAIGSTTFLIINSIQAIMETKLKWQDKIDDKKSNRTVLGGGRKYGGKKWWKFG
FGGGVSSSWFSGSTVSSKLSSLAPSNWGGSSVGR

Enzyme Prediction     

EC	2.4.1.16:26	2.4.1.16:26

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	1114	1276	1.7e-79	0.9938650306748467
GT2	1254	1482	6.9e-21	0.4098671726755218

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
236223	PRK08294	2.71e-120	1	585	45	603	phenol 2-monooxygenase; Provisional
396286	Chitin_synth_1	4.51e-114	1114	1276	1	163	Chitin synthase. This region is found commonly in chitin synthases classes I, II and III. Chitin a linear homopolymer of GlcNAc residues, it is an important component of the cell wall of fungi and is synthesized on the cytoplasmic surface of the cell membrane by membrane bound chitin synthases.
133033	Chitin_synth_C	1.07e-91	1110	1430	1	244	C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin. Chitin synthase, also called UDP-N-acetyl-D-glucosamine:chitin 4-beta-N-acetylglucosaminyltransferase, catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of GlcNAc residues formed by covalent beta-1,4 linkages. Chitin is an important component of the cell wall of fungi and bacteria and it is synthesized on the cytoplasmic surface of the cell membrane by membrane bound chitin synthases. Studies with fungi have revealed that most of them contain more than one chitin synthase gene. At least five subclasses of chitin synthases have been identified.
400366	Phe_hydrox_dim	3.89e-58	404	582	1	166	Phenol hydroxylase, C-terminal dimerization domain. Phenol hydroxylase acts a homodimer, to hydroxylates phenol to catechol or similar product. The enzyme is comprised of three domains. The first two domains from the active site. The third domain, this domain, is involved in forming the dimerization interface. The domain adopts a thioredoxin-like fold.
396193	FAD_binding_3	3.01e-47	1	368	14	348	FAD binding domain. This domain is involved in FAD binding in a number of enzymes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAE7175496.1|GT2	0.0	715	1834	1	1122
QRD06573.1|GT2	0.0	715	1834	95	1130
CAB41508.1|GT2	0.0	885	1834	1	967
CBX90656.1|GT2	0.0	927	1794	1	862
UJO15676.1|GT2	0.0	726	1793	7	1095

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1PN0_A	7.89e-162	12	607	37	641	Phenol hydroxylase from Trichosporon cutaneum [Cutaneotrichosporon cutaneum],1PN0_B Phenol hydroxylase from Trichosporon cutaneum [Cutaneotrichosporon cutaneum],1PN0_C Phenol hydroxylase from Trichosporon cutaneum [Cutaneotrichosporon cutaneum],1PN0_D Phenol hydroxylase from Trichosporon cutaneum [Cutaneotrichosporon cutaneum]
1FOH_A	2.77e-159	12	607	36	640	Phenol Hydroxylase From Trichosporon Cutaneum [Cutaneotrichosporon cutaneum],1FOH_B Phenol Hydroxylase From Trichosporon Cutaneum [Cutaneotrichosporon cutaneum],1FOH_C Phenol Hydroxylase From Trichosporon Cutaneum [Cutaneotrichosporon cutaneum],1FOH_D Phenol Hydroxylase From Trichosporon Cutaneum [Cutaneotrichosporon cutaneum]
2DKH_A	2.81e-76	12	585	57	609	Crystal structure of 3-hydroxybenzoate hydroxylase from Comamonas testosteroni, in complex with the substrate [Comamonas testosteroni],2DKI_A Crystal structure of 3-hydroxybenzoate hydroxylase from Comamonas testosteroni, under pressure of xenon gas (12 atm) [Comamonas testosteroni]
4ICY_A	2.73e-15	302	440	276	418	Tracing the Evolution of Angucyclinone Monooxygenases: Structural Determinants for C-12b Hydroxylation and Substrate Inhibition in PgaE [Streptomyces sp. PGA64]
2QA1_A	2.73e-15	302	440	276	418	Crystal structure of PgaE, an aromatic hydroxylase involved in angucycline biosynthesis [Streptomyces sp. PGA64]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q92444|CHS2_PARBR	0.0	903	1771	79	975	Chitin synthase 2 OS=Paracoccidioides brasiliensis OX=121759 GN=CHS2 PE=3 SV=2
sp|P30600|CHS1_EXODE	0.0	868	1826	30	977	Chitin synthase 1 OS=Exophiala dermatitidis OX=5970 GN=CHS1 PE=3 SV=2
sp|P30584|CHSA_EMENI	0.0	859	1772	22	959	Chitin synthase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=chsA PE=3 SV=2
sp|P30589|CHS2_NEUCR	0.0	909	1770	152	1060	Chitin synthase 2 OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=chs-2 PE=3 SV=4
sp|P87073|CHS1_PHYB8	1.26e-282	1022	1759	89	837	Chitin synthase 1 OS=Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC 33097 / NRRL 1555) OX=763407 GN=chs1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000068	0.000000

TMHMM  Annotations     

Start	End
1458	1480
1501	1523
1533	1555
1568	1590
1605	1624
1699	1721
1736	1758