ID R9JID6_9FIRM Unreviewed; 3413 AA.
AC R9JID6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Pullulanase, type I {ECO:0000313|EMBL:EOS34019.1};
GN ORFNames=C804_01764 {ECO:0000313|EMBL:EOS34019.1};
OS Lachnospiraceae bacterium A4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=397291 {ECO:0000313|EMBL:EOS34019.1, ECO:0000313|Proteomes:UP000014118};
RN [1] {ECO:0000313|EMBL:EOS34019.1, ECO:0000313|Proteomes:UP000014118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4 {ECO:0000313|EMBL:EOS34019.1,
RC ECO:0000313|Proteomes:UP000014118};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium A4.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOS34019.1}.
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DR EMBL; ASSR01000034; EOS34019.1; -; Genomic_DNA.
DR STRING; 397291.C804_01764; -.
DR PATRIC; fig|397291.3.peg.1805; -.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG1196; Bacteria.
DR eggNOG; COG1523; Bacteria.
DR eggNOG; COG3209; Bacteria.
DR HOGENOM; CLU_000318_0_0_9; -.
DR OrthoDB; 9761875at2; -.
DR Proteomes; UP000014118; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0051060; F:pullulanase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11341; AmyAc_Pullulanase_LD-like; 1.
DR CDD; cd10315; CBM41_pullulanase; 1.
DR CDD; cd02859; E_set_AMPKbeta_like_N; 2.
DR CDD; cd02860; E_set_Pullulanase; 1.
DR Gene3D; 2.60.40.1110; -; 1.
DR Gene3D; 1.20.1270.70; Designed single chain three-helix bundle; 7.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR005323; CBM41_pullulanase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004193; Glyco_hydro_13_N.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR011840; PulA_typeI.
DR NCBIfam; TIGR02104; pulA_typeI; 1.
DR PANTHER; PTHR43002; GLYCOGEN DEBRANCHING ENZYME; 1.
DR Pfam; PF00128; Alpha-amylase; 4.
DR Pfam; PF02922; CBM_48; 1.
DR Pfam; PF07554; FIVAR; 6.
DR Pfam; PF03714; PUD; 1.
DR SMART; SM00642; Aamy; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF81296; E set domains; 3.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000014118};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..3413
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038629972"
FT DOMAIN 904..1274
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 1800..2202
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 50..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2731..2758
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 50..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3413 AA; 377881 MW; BBA77AF6E9520789 CRC64;
MEKAKTFCRK KRNLAKSMLS LMLVFAMVIS NVQITPDAFS TVWAAENETL ETSEASENSS
QPSEAAGDSE EAGEASENSG DDKDTGTEET GKPTQESEAG SSLREEDFAQ SEAVTETEAS
KQTDEEDSTK ETTTTNASTE NSEDSDSVDS STQSVVEETS EDANDSTAQE TETITETTES
MTTEEATETE TAEDENISAD EAVGEAVDVV VHFKNTLNWN AVRLHSWIRN NGKDTNFFEE
NAGKLLEERE GYYSYTFENI ILEDSFEFIG FLINASKEDI WAANNFQTTN ITISKSELSN
TENGKYECWV WLIDGNRDGE NKTIPQVSKL GLDGPEISSD GTQVTFRYQN ADASQVTIKG
VKGDVWNNDT EVIEQVMDKD SNTGIFTSTV NLPKEGFSYK FVVKYEGNDN ENWIFDPSNQ
NIVNGNSYVR KAAEKAVIRF HFKNALNWET ISMHYWGMGI DGSDWPGAPL DLSDSNKDEK
EFYTFDVNAD GLIHDLGFIV TDGKADGGLQ TTDNTISRSS IPDNDTYELW IWLDENKKDE
GKYIPCISTS PISSPEFGET TENGTEVTFR YQQESGSAAK VLLAGTMTDW LEEPVEMSKD
ENDIWSCTMT LPHGEYEYKY VIPKEGETDP GTDGSKYNWE FDPFNTNYST HKENDQVIKD
NSLVYVAGEE YTYTVHYYNP ANKASTADES DLYIWEPGIT YTDTAKVWKY ESIETDTNGI
PWQTVSFKVP YKAMGIIGRP TAGSWTGQDT NQYYQLKQIR NGNVVENKTA EFWYIHGQGI
YATAPELGGV TNLSASFDGN ASMDYTQNKV LHIDATDSEN NKVFVKEAYV NASGLGISEK
LFIDPELMEV TLSVTEDTPY GDVELPITVV DYQGNTIKTS VTVKVVAKTE SENDFDWDEA
VIYFMVTDRF KDGDASNNEK AGADTFNKNN PGLYHGGDFA GVKEHLNDLK NLGVNTIWIT
PIVKNIPKVQ VDDGTGPIPN YASYHGYWAS DFSDINGALG TREEFQDLIN AVHAENMKLM
VDVVVNHAGY GAEESETFSG MLREAAIEDD AFHGGGGQAG LPDFMTENPE VRDMIIGWQL
EWAEMGVDYF RVDTVKHVDN TTWMAFKNAL TKADPDFKMI GEYYGASYNS ENGGTLGSGE
MDSLLDFNFK YQAGNFVRGG ISSVETELQK RNAALNNTYL LGQFLSSHDE NGFKFNLKQG
ENKMSDAAAD AAALVAATLQ ITAKGQPVIY YGEEIGLTGE NNYPQQTNRY DYDWTINKET
SATYQHYKNL LGIRQKYSEI FARGDRKVVT LSDSGKYDVI SRSYNGETIY VGMNINPDQA
VDNLEIQVNN EGITQYKDEY SGNTYSVKDG KITITIPKAS EGGTVVLVPS GFNDTLVAPQ
ISTIAKGKTT LLPSQLTHIA EDGTKSPVEV TYSINNSADG VSLDDTKTKL TVSETFEGTE
IQLTATSESA GSVTFTVKAV EDKNEITVKI HYTRDDGNYD EWNVWAWPEG KGGAQYDFTS
ENDEMVTVAK FEGRSISRLG YRIRKGDWAE NDPIEVDRYI DLSNILSGTI HYYVKSGVYD
GTMVMEEDVL LGSKVISAKY NQSTKRIEVV LGGNDAVGNI SELFAIKDYS NTEIPITNVT
KRRDMYVLTI DKDLSAIDDL VKSYFVAFDG YDYKITMPVA YSSAEFENKY TYEGDDLGAT
WTKDKTTFKV WAPTADKVEV KLYKSGTEGL DDLIDTLDME KSNNGVWVLE KDGDLNGTYY
TYNVYVDGTE IEACDPYART TGVNGNRAMV INLDATNPEG WAADRGPNAD MSYTDSIIYE
LHVRDFSIKE NSGISDEHKG KFLGLIESGT TNGNGQPTGL DYLTDLGVTH IHLLPSYDYT
TVDETKLDTP QFNWGYDPKN YNVPEGSYST DPYNGEVRVK EMKQMIKTLH DNNINVIMDV
VYNHVYDADK FCFNQIVPKY FSRTNADGTY SNGSGCGNDT ASERAMVKKY IVDSVNYWAE
EYHIDGFRFD LVGLLDTKTI NEVVETVHKR HPEAVFYGEG WALNTAVSKD GYTMATQANA
SATPKFAYFS DTIRDLVKGK NDEENLGFVS GLTGKEEDMA NCFRSLTWWS KNPTQIVNYA
SCHDNYTLMD KLYATTERKG NASRAEVIKM NNLSAAIYMM AEGIPLIHAG EEILRIKRDE
KDNIIHNSYN SPDSVNQIKW EDLDKPEYRA VRDYYKGLID FRKNHAALRL DSADAVAANV
KYHWVTNEVI LFAINGKDSV PDEVSDGIVI IFNATKTDQD VNLYEYGIKE DETWNVCINE
KEAGTKVLSQ VTDGTVKVAP ISAMVLVKGE TVDANSVYEE NKLQNTERQR KYLQDLISRC
EKLVPDNYTE ESWNVFQEAL LSAKQVWESA TATQEQLIDA RENLTAAYDA LEVIAGVVDT
AKLDALIAEC KEKVAGGQGE YTTESWTVFT EALSAAEAVR AEQEVTQEAI NAAYDSLKAA
YEGLKKPVAN TDKLKELIKE YDNLKQGNYT DESWAVFVNA LAAAKAAVAK PDATQAEIDK
AEQDLRDAYS ALKVPEGTVD KEKLKALVAI YKEIQNAGQG DYTDESWKAF SDELANAEAL
LEKSDATQAE IDEAYSKLET AYTNLTSTKN TEKLDELIAE CSKLDKGDYT DESWNALQEA
LKAAKEIADK PNATQAEIDK AEQDLRDAYN ALKVPEGTID KGKLKALIAV CDEILNKGQG
SYTAESWNAF TLALEEAKAI LAKEDATQPE VDEARNKLDK AHNNLVSIEE EIKALKELIV
TCEKYIKEDY TTESWRVFED ALQAAKEVAE NPNAALEEIQ RAADDLQNAV KALIKVKEGL
WTAWAPDSGL TAPENGEGNY HAAYTGKAFK PEILVYDGKT LLKEKTDYTV SYKNNTNAGP
ATVTVKGKGN YSESTTAEFT IDPIDIATLE IEDLYAAVAS NNTKQVALKP IVKFNGKTLK
MGKDYTVAYA DPNGGKAPGN PSMDYDVKID AASVNFTGTK MIKMTLVDKD NAYLMSKASI
GKIVTADRVY TGEVLKPQIT VKYGKTTLVK DTDYTVLYDN EHIEAGETAT ITIRGNGTTY
FGEKTTSFKI TGTPLKAGQI SLKDVPKTGL VYTGKPQEPE IDGIDKKNYE AVYQNNTNAG
TATVVITGKN GYTGTVKKTF KITAYDIFAN SDKKFKYNIN GSIPFAKGGS KLTDDQTGAR
FTISDGVEIT LQQGKDYTLS YKNNKKVGDN TASVTIKGKG NFKGTLKNIP FTIVAQDLSN
LNITAADVLQ KNAKKFNKVV PVVTDLDGKT LKNKTDFELD TATAYTDEAG NPISSTEPAT
GTAIKVTVTG KGNYQGTASA IFHIIDNNMS IAKASVQIEP QRYTGSEVTL SNDQIHVKLK
INGTITELQN DNFQIVGYSK NIKKGTAKVT IRGIYPYGGT KTVNFKITAR PMN
//
