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Protein

Cyclomaltodextrin glucanotransferase

Gene

cgt

Organism
Bacillus sp. (strain 1-1)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic activityi

Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)-alpha-D-glucosidic bond.

Cofactori

Ca2+By similarityNote: Binds 2 calcium ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi52Calcium 1By similarity1
Metal bindingi54Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi57Calcium 1By similarity1
Metal bindingi58Calcium 1By similarity1
Metal bindingi76Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi78Calcium 1By similarity1
Metal bindingi161Calcium 2By similarity1
Binding sitei162SubstrateBy similarity1
Metal bindingi212Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi221Calcium 2By similarity1
Binding sitei249SubstrateBy similarity1
Active sitei251NucleophileBy similarity1
Metal bindingi255Calcium 2; via carbonyl oxygenBy similarity1
Active sitei279Proton donorBy similarity1
Binding sitei349SubstrateBy similarity1
Sitei350Transition state stabilizerBy similarity1
Binding sitei393SubstrateBy similarity1
Binding sitei397SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosyltransferase, Transferase
LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.19 691

Protein family/group databases

CAZyiCBM20 Carbohydrate-Binding Module Family 20
GH13 Glycoside Hydrolase Family 13

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclomaltodextrin glucanotransferase (EC:2.4.1.19)
Alternative name(s):
Cyclodextrin-glycosyltransferase
Short name:
CGTase
Gene namesi
Name:cgt
OrganismiBacillus sp. (strain 1-1)
Taxonomic identifieri29334 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 291 PublicationAdd BLAST29
ChainiPRO_000000143830 – 703Cyclomaltodextrin glucanotransferaseAdd BLAST674

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi68 ↔ 75By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP31746
SMRiP31746
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini520 – 598IPT/TIGAdd BLAST79
Domaini599 – 703CBM20PROSITE-ProRule annotationAdd BLAST105

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni30 – 160A1Add BLAST131
Regioni122 – 123Substrate bindingBy similarity2
Regioni161 – 224BAdd BLAST64
Regioni215 – 218Substrate bindingBy similarity4
Regioni225 – 428A2Add BLAST204
Regioni254 – 255Substrate bindingBy similarity2
Regioni429 – 516CAdd BLAST88
Regioni517 – 600DAdd BLAST84
Regioni601 – 703EAdd BLAST103

Domaini

May consist of two protein domains: the one in the N-terminal side cleaves the alpha-1,4-glucosidic bond in starch, and the other in the C-terminal side catalyzes other activities, including the reconstitution of an alpha-1,4-glucosidic linkage for cyclizing the maltooligosaccharide produced.

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.10, 2 hits
2.60.40.1180, 1 hit
InterProiView protein in InterPro
IPR031319 A-amylase_C
IPR006046 Alpha_amylase
IPR013784 Carb-bd-like_fold
IPR002044 CBM_fam20
IPR006047 Glyco_hydro_13_cat_dom
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
IPR002909 IPT_dom
PfamiView protein in Pfam
PF00128 Alpha-amylase, 1 hit
PF00686 CBM_20, 1 hit
PF01833 TIG, 1 hit
PRINTSiPR00110 ALPHAAMYLASE
SMARTiView protein in SMART
SM00642 Aamy, 1 hit
SM00632 Aamy_C, 1 hit
SM01065 CBM_2, 1 hit
SUPFAMiSSF49452 SSF49452, 1 hit
SSF51445 SSF51445, 1 hit
SSF81296 SSF81296, 1 hit
PROSITEiView protein in PROSITE
PS51166 CBM20, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P31746-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNDLNDFLKT ILLSFIFFLL LSLPTVAEAD VTNKVNYSKD VIYQIVTDRF
60 70 80 90 100
SDGNPGNNPS GAIFSQNCID LHKYCGGDWQ GIIDKINDGY LTDLGITALW
110 120 130 140 150
ISQPVENVYA LHPSGYTSYH GYWARDYKKT NPYYGNFDDF DRLMSTAHSN
160 170 180 190 200
GIKVIMDFTP NHSSPALETN PNYVENGAIY DNGALLGNYS NDQQNLFHHN
210 220 230 240 250
GGTDFSSYED SIYRNLYDLA DYDLNNTVMD QYLKESIKFW LDKGIDGIRV
260 270 280 290 300
DAVKHMSEGW QTSLMSEIYS HKPVFTFGEW FLGSGEVDPQ NHHFANESGM
310 320 330 340 350
SLLDFQFGQT IRNVLKDRTS NWYDFNEMIT STEKEYNEVI DQVTFIDNHD
360 370 380 390 400
MSRFSVGSSS NRQTDMALAV LLTSRGVPTI YYGTEQYVTG GNDPENRKPL
410 420 430 440 450
KTFDRSTNSY QIISKLASLR QTNSALGYGT TTERWLNEDI YIYERTFGNS
460 470 480 490 500
IVLTAVNSSN SNQTITNLNT SLPQGNYTDE LQQRLDGNTI TVNANGAVNS
510 520 530 540 550
FQLRANSVAV WQVSNPSTSP LIGQVGPMMG KAGNTITVSG EGFGDERGSV
560 570 580 590 600
LFDSTSSEII SWSNTKISVK VPNVAGGYYD LSVVTAANIK SPTYKEFEVL
610 620 630 640 650
SGNQVSVRFG VNNATTSPGT NLYIVGNVNE LGNWDADKAI GPMFNQVMYQ
660 670 680 690 700
YPTWYYDISV PAGKNLEYKY IKKDQNGNVV WQSGNNRTYT SPTTGTDTVM

INW
Length:703
Mass (Da):78,663
Last modified:July 1, 1993 - v1
Checksum:i4D973FB21D0D9B0A
GO

Sequence databases

PIRiS26399 ALBSX1

Similar proteinsi

Entry informationi

Entry nameiCDGT_BACS2
AccessioniPrimary (citable) accession number: P31746
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: February 28, 2018
This is version 104 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

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