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CAZyme Information: MGYG000000977_00398

You are here: Home > Sequence: MGYG000000977_00398

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Clostridium sp900539375
Lineage Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium sp900539375
CAZyme ID MGYG000000977_00398
CAZy Family GH13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1197 136074.15 5.7805
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000977 2927434 MAG Australia Oceania
Gene Location Start: 12681;  End: 16274  Strand: -

Full Sequence      Download help

MKKISIIFLA  VILFSNIINC  LTVRAIINDE  EIKIAKENLK  DEIILNACNY  SLENIIGKLE60
EIDKAGYSII  EISPIQGTKS  DDLDGSKWWL  LSQPINQDIG  NAQIGNKDDL  INLCTEAKKT120
GIKIIVQVEL  NHMAFSEDNE  TLSELVVEEF  KDIDLYHDLG  KCDDWSNRWA  VTQKNIKGMD180
LNTQNPNVQE  KALKFLNDCI  DAGVSGFRFN  KANYIETSYG  EDLEKGWASD  YWEYILGNLK240
NKESLLIYGD  IKNCDANNED  AYKKYMNISS  EKYADSLLEA  VRSNKLKNID  INNKISSQYF300
ENEDSFYLGE  SKNLSENERK  ICWAILSARK  DVSPIFFSRP  SNKIGNIGED  FYNHEDIKVL360
NKFHKDMKGL  SENIRLINDN  AMLIERGRNG  AVLVNNGEHA  VINIETNLED  GMYENKISDG420
GTFVVSNGRL  IGNIKKKTVA  VFYKEKIVYF  KSPSNWNEAS  IYVYKNKEEL  SEWPGKKMIY480
DNNKGLYYYI  FPEGWNEEAV  RVIFNNRGDV  LNQLENQIPQ  TGKQGFLCDK  VTSIFDSSKE540
YKEGQSLEYY  SKDGFFIGGL  TTDKSSPQTI  NKEIKIYAGA  SGCSGKIQYE  FYEKLNGKEI600
IIRNYSEQNN  ASWNPRTVGM  YILGVRAKNE  NGEIIRKEIN  YEIKDELSIT  NFSIDCMSPQ660
EIKKTINISA  DSIGGTGKIL  YKFYIKDKNE  TKILQDFNEN  KTVKWVPDIP  GNYKIIVEVK720
DSTGNIVKNE  KSDFVINDKL  KINTFDTNYI  NGQEIGKKVL  LTGNASGGNG  DILYKFLYKK780
DNTYKLIRDF  DTENTVTWIP  ETSGNYKLIL  KVKDKNSKEI  EKVIENYNVS  ESIKITNFSL840
SKDGNGVDIQ  AKASGGVGKL  KYKFVAKYDD  EYEIIQDYSE  NNMVKWLPQK  NNVTCTLTVQ900
IKDENGNIIN  KIIDRYFIGE  SIYIDSFTTD  KTSPQVSGTK  VILKVEASGE  GTLQYKFLIK960
DNKTGNWAVL  REYGTSNTYT  WATKTIGDKT  LYVDVKDSTG  KVVRSQMSYK  VIKPLVISSF1020
IADKESPQIS  ETKVPLKVEA  SGEGILQYKF  LIKDNKTGNW  ALLRDYGTSN  TYTWTTKTTG1080
DKTLYVDVKD  STGKVVRSQM  SYKVIKPLVI  SSFIADKESP  QISGTKVTLK  VEASGEGTLQ1140
YKFLIKDSLG  NWALLRDYGT  FNSYVWTTKQ  TGDKTLYVDV  KDENEQVVRD  SIKYIVK1197

Enzyme Prediction      help

No EC number prediction in MGYG000000977_00398.

CAZyme Signature Domains help

Created with Snap5911917923929935941847853859865871877883789795710171077113751295GH13
Family Start End Evalue family coverage
GH13 51 295 7.1e-64 0.9022556390977443

CDD Domains      download full data without filtering help

Created with Snap5911917923929935941847853859865871877883789795710171077113741374AmyAc_bac1_AmyA6511090PRK140815631066PRK140817691184PRK140818581195PRK14081
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11315 AmyAc_bac1_AmyA 4.03e-86 41 374 1 352
Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes Firmicutes, Proteobacteria, Actinobacteria, and Cyanobacteria. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
PRK14081 PRK14081 1.97e-35 651 1090 5 458
triple tyrosine motif-containing protein; Provisional
PRK14081 PRK14081 8.43e-28 563 1066 9 625
triple tyrosine motif-containing protein; Provisional
PRK14081 PRK14081 1.05e-27 769 1184 29 460
triple tyrosine motif-containing protein; Provisional
PRK14081 PRK14081 2.85e-27 858 1195 30 373
triple tyrosine motif-containing protein; Provisional

CAZyme Hits      help

Created with Snap5911917923929935941847853859865871877883789795710171077113738632QES71965.1|CBM25|GH13_2838632AVK49730.1|CBM25|GH13_2838632AQS03274.1|CBM25|GH13_2838632AJG97367.1|CBM25|GH13_2838632CUU45913.1|CBM25|GH13_28
Hit ID E-Value Query Start Query End Hit Start Hit End
QES71965.1 1.93e-111 38 632 48 651
AVK49730.1 2.68e-111 38 632 48 651
AQS03274.1 9.98e-111 38 632 48 651
AJG97367.1 2.60e-110 38 632 48 650
CUU45913.1 5.17e-110 38 632 48 651

PDB Hits      download full data without filtering help

Created with Snap59119179239299359418478538598658718778837897957101710771137384451BAG_A384453DC0_A384451UA7_A662181KXH_A662181G94_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
1BAG_A 1.78e-55 38 445 5 425
ChainA, ALPHA-1,4-GLUCAN-4-GLUCANOHYDROLASE [Bacillus subtilis]
3DC0_A 3.04e-55 38 445 2 422
Crystalstructure of native alpha-amylase from Bacillus sp. KR-8104 [Bacillus sp. KR-8104]
1UA7_A 5.60e-55 38 445 2 422
ChainA, Alpha-amylase [Bacillus subtilis]
1KXH_A 8.34e-10 66 218 28 182
ChainA, alpha-amylase [Pseudoalteromonas haloplanktis]
1G94_A 3.36e-09 66 218 28 182
CRYSTALSTRUCTURE ANALYSIS OF THE TERNARY COMPLEX BETWEEN PSYCHROPHILIC ALPHA AMYLASE FROM PSEUDOALTEROMONAS HALOPLANCTIS IN COMPLEX WITH A HEPTA-SACCHARIDE AND A TRIS MOLECULE [Pseudoalteromonas haloplanktis],1G9H_A TERNARY COMPLEX BETWEEN PSYCHROPHILIC ALPHA-AMYLASE, COMII (PSEUDO TRI-SACCHARIDE FROM BAYER) AND TRIS (2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL) [Pseudoalteromonas haloplanktis],1L0P_A Crystal Structure Analysis Of The Complex Between Psychrophilic Alpha Amylase From Pseudoalteromonas Haloplanctis And Nitrate [Pseudoalteromonas haloplanktis]

Swiss-Prot Hits      download full data without filtering help

Created with Snap5911917923929935941847853859865871877883789795710171077113737445sp|P23671|AMY_CLOAB38447sp|P00691|AMY_BACSU34457sp|P30269|AMY_BUTFI66215sp|P29750|AMY_THECU66241sp|O76284|AMYR_DROBC
Hit ID E-Value Query Start Query End Hit Start Hit End Description
P23671 2.74e-103 37 445 49 463
Alpha-amylase OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=amyA PE=3 SV=2
P00691 7.93e-53 38 447 46 468
Alpha-amylase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyE PE=1 SV=2
P30269 6.62e-33 34 457 140 625
Alpha-amylase OS=Butyrivibrio fibrisolvens OX=831 GN=amyA PE=3 SV=1
P29750 2.82e-12 66 215 65 224
Alpha-amylase OS=Thermomonospora curvata OX=2020 GN=tam PE=1 SV=1
O76284 2.00e-11 66 241 56 227
Alpha-amylase-related protein OS=Drosophila bocqueti OX=74549 GN=Amyrel PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.001014 0.996281 0.002124 0.000199 0.000176 0.000176

TMHMM  Annotations      download full data without filtering help

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