ID Q13FE3_PARXL Unreviewed; 2868 AA.
AC Q13FE3;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 10-JUN-2026, entry version 104.
DE SubName: Full=Cyclic beta 1-2 glucan synthetase {ECO:0000313|EMBL:ABE37196.1};
DE EC=2.4.1.20 {ECO:0000313|EMBL:ABE37196.1};
GN ORFNames=Bxe_C1346 {ECO:0000313|EMBL:ABE37196.1};
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE37196.1, ECO:0000313|Proteomes:UP000001817};
RN [1] {ECO:0000313|EMBL:ABE37196.1, ECO:0000313|Proteomes:UP000001817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400 {ECO:0000313|EMBL:ABE37196.1,
RC ECO:0000313|Proteomes:UP000001817};
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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DR EMBL; CP000272; ABE37196.1; -; Genomic_DNA.
DR RefSeq; WP_011494422.1; NC_007953.1.
DR STRING; 266265.Bxe_C1346; -.
DR KEGG; bxe:Bxe_C1346; -.
DR PATRIC; fig|266265.5.peg.9100; -.
DR eggNOG; COG3459; Bacteria.
DR OrthoDB; 9769991at2; -.
DR Proteomes; UP000001817; Chromosome 3.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0047738; F:cellobiose phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11756; GH94N_ChvB_NdvB_1_like; 1.
DR CDD; cd11753; GH94N_ChvB_NdvB_2_like; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 1.50.10.140; -; 2.
DR Gene3D; 2.70.98.40; Glycoside hydrolase, family 65, N-terminal domain; 2.
DR Gene3D; 2.60.420.10; Maltose phosphorylase, domain 3; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR037018; GH65_N.
DR InterPro; IPR033432; GH94_catalytic.
DR InterPro; IPR052047; GH94_Enzymes.
DR InterPro; IPR037824; GH94N_2_NdvB.
DR InterPro; IPR037820; GH94N_NdvB.
DR InterPro; IPR010383; Glyco_hydrolase_94_b-supersand.
DR InterPro; IPR019282; Glycoamylase-like_cons_dom.
DR PANTHER; PTHR37469:SF2; CELLOBIONIC ACID PHOSPHORYLASE; 1.
DR PANTHER; PTHR37469; CELLOBIONIC ACID PHOSPHORYLASE-RELATED; 1.
DR Pfam; PF06165; GH94_b-supersand; 2.
DR Pfam; PF17167; Glyco_hydro_94; 1.
DR Pfam; PF10091; Glycoamylase; 1.
DR SMART; SM01068; CBM_X; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 2.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:ABE37196.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABE37196.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 410..435
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 441..458
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 822..839
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 845..867
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 949..967
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1301..1498
FT /note="Glycoamylase-like"
FT /evidence="ECO:0000259|Pfam:PF10091"
FT DOMAIN 1563..1830
FT /note="Glycosyl hydrolase 94 supersandwich"
FT /evidence="ECO:0000259|Pfam:PF06165"
FT DOMAIN 2067..2337
FT /note="Glycosyl hydrolase 94 supersandwich"
FT /evidence="ECO:0000259|Pfam:PF06165"
FT DOMAIN 2350..2777
FT /note="Glycosyl hydrolase 94 catalytic"
FT /evidence="ECO:0000259|Pfam:PF17167"
FT REGION 2013..2044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2032..2041
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2868 AA; 313504 MW; 48AE889BBBC61A8C CRC64;
MKTILRYIAG RRLPSPPWTD IAPVREELFG VERIEQHAES LAAAQPVTKT PPAVLSLHTR
LNDNAAVLLA AYRASAAELE SGRGVVPAAE WLLDNYHLVE TQIREIRDDL PPGYYRQLPK
LAAGPFAGYP RVFGLAWAFV AHTDSHFDPQ ILRRFISAYQ RVQPLTIGEL WAVAITLRIV
LIENLRRLAD QITAGRSARA DADALTERLL ESGGARSALE ADIATRSTDL LSELFAAQLA
KRLRDRDPCT MPALGWLEER LRLQGASIEQ VVQHAQQRQG ASNVTVRNVI TSMRLISDID
WAELFEEVSL VDARLRAGSR FATMDFPTRN LYRSAIEQLA RGSSFTELEV AGLALESARA
AAQASGDAAQ AERAGDPGYH LIAEGRQALE QAIGFRPPAR LRITRFNVQL GIGGYVGTIL
AVAATLLALV LWAMWILAPS GLAPLVFALF AACGFLPVTE IATALVNRAV TWSFGAITLP
GLELTAGVPS SLRTLVAVPT LLTSEADLRE QIERLEVHHL AGAGGDLSFA LLADGLDANQ
EVLPSDAHLL AVAADAIEAL NRRYEPSPGG NRFLLLHRRR VFNASENRWM GWERKRGKLH
ELNRLLRGAT DTTFMPIAGR APQVPSDVRY VITLDADTRL PRDAALRLIG KMAHPLNRPT
FSDAEQRVVN GYAILQPRVT PSLPVGQEGS LHQRVFSGPG GMDPYAAAVS DVYQDLFGEG
SYTGKGIYDV DAFEAALHGR VPENALLSHD LFEGIFARAG LASDVEVVEE VPSRYDVIGK
RQHRWTRGDW QLLPWIVGHR GSDRHAMPSI GRFKMLDNLR RSLLAPFMVA ALGLCWLMPL
RAGIAGALLV LGALAIPAFL PTLFAILPRR SGVRLRNHLD VLAADVRLAA MQTFLSTAFL
ADHAWRMGDA IVRTLTRLFV THRRLLEWTT AAQSTGSPRL DLRGFYRQMA GSVALCVVLT
AGAIALAPSH WPLVLPFALL WLAAPTFALW SSRSPTVARR FTMTDPDTRS LRLIARRTWR
FFETFVTAAE NMLPPDNFQE DPAPVVAHRT SPTNLGLYLL SAIAARDFGW AATTQTVERL
EATFASMHKL ARFKGHFYNW YGTLDLQVLA PAYVSSVDSG NLAGHLIAVA NACEEWQHDL
LAPAARSGMV DNLQLARAAI DALPAAGGER GTHLVGILEE IRAQLHGPQT LDALSPLLMR
LTEKAGKATR ELVPAGGDAS SADLMFWVDA LSKSLVEHAR DRQQFAEAPS LLQARLKSLA
DTSRALALDM DFAFLLDPER KLLSIGYSQA DNSLDLNCYD LLASEARLAS LFAIAKGDVT
TRHWFRLGRA ATPVGKGSAL ISWSGSMFEY LMPSLVMRAP AGSLLEQTNR LVVERQVSYG
RSLGIPWGIS ESAYNARDIE FTYQYSNFGV PGLGLKRGLS ENRVIAPYAT GLAAMVNPQA
ALENYGQLAA LGALGRYGFY EALDFTRSRL PDNADVAIVR NFMAHHQGMT IVSIANTLLD
ARMRARFHRE PMIQASELLL QERMPRNVAV GHPRAEEVNT AAAVSGAAPS TVRRLAASAV
AGAAPVTHLL SNGHYAVMLT ATGAGYSRWR DLAVTRWRED ATRDDWGSFI FLRDTQSGHA
WSAGAQPVGS EADYEEVVFG EDHAEFIRRD GSLTTTMDVL VSGEADGEVR RVSLANSGRR
AREIELTSYA EIVLATPASD NAHPAFSRMF VQTEHVAEFG ALLATRRPRS HDEKQVWAAH
FAVVDGEIIA DPQYESDRAR FLGRGRSAGT AAAIFDDQPL TNTAGTVLDP VFALRYRVLV
PPGKVARVTF WTVVAESRAL LLDLVDQHHD RNAFDRAKTL AWTQAQVQLR HLDVEAEEAA
DFQRLAAPVI YADARFRAQS DTIVRGAGVQ SGLWPHAISG DLPIVLLRID EVEDIAQVRQ
LLRAHEYWRM KRLDVDLVII NERASSYIQE LQGAIETAVR SSQSRPRFGE ELAHGAVFTL
RAELMSMEAR ALLQSVARVA LIARRGSIAD QLARLPQSQG QPSALRRQKP PMSSPWPAPP
HLPRELSSVP SSLEFFNGLG GFGKNGREYV TVLTAGATTP APWINVIANP DFGFQVAAEG
SGYTWAENSR ENQLTPWSND PVEDPAGEAI YVRDEITGEV WGATAQPIRD GGIYVARHGH
GYSRFEHDAN GIALDLLQYV PLADPLKISR LTLRNLSARP RRLSVTAWTE WVLGTSRGAS
GPFIVTEIDS ATGAMLARNP WSMGFAGRVA FADLGGRQTA WTADRTEFLG RNGRGAAPAA
LSGNARLSGA TGAGLDPCAA LQDVIELGVG EIVEVVSFVG QCASAEQARA LIERYRKADL
DAVLAEVTSH WRNVLGAIQV KTPDRAMDLM LNGWLLYQTL ACRIWARSAF YQASGAYGFR
DQLQDGMALT HVRPDETRRH LLRAAARQFV EGDFQHWWLP QTGQGVRTRI SDDRVWLAFA
TATYVRCAGD VAILDEIVPF LDGPLLRPGE HDAFFQPMVA DESASLFEHC ARGLDQCIEL
TGAHGLPLIG TGDWNDGMNG VGAGGNGESV WLGWLLLRTV ELFAPLAELR DPAAVARAAR
WRAHAASLRE SLERDAWDGQ WYRRATFDDG RWLGSNDSDE CQIDSIAQSW AVLSGAADPA
HAALAMASLE KHLIRHDDAL ALLFTPPFDK TSHDPGYIKG YPPGLRENGG QYSHAAMWAV
LALTGLGEGN KAAALFSLLN PINHARTPLE VDRYKVEPYV VAADVYSVAP HAGRGGWTWY
TGSAGWMYRA GVEGILGVCR EGDFLVVDPC IPDTWPGFEA TVTMHSTRYE VRVESADGGD
AMRVMLDGAS LECGDERVRV PLDGGSHKLL ISRCFGVSED MNSNAQVA
//
