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Database: UniProt
Entry: R6PLX5_9FIRM
LinkDB: R6PLX5_9FIRM
Original site: R6PLX5_9FIRM 
ID   R6PLX5_9FIRM            Unreviewed;      1393 AA.
AC   R6PLX5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Multimodular carbohydrate-active enzyme {ECO:0000313|EMBL:CDC19426.1};
GN   ORFNames=BN582_00245 {ECO:0000313|EMBL:CDC19426.1};
OS   Eubacterium sp. CAG:274.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=1262888 {ECO:0000313|EMBL:CDC19426.1, ECO:0000313|Proteomes:UP000017904};
RN   [1] {ECO:0000313|EMBL:CDC19426.1, ECO:0000313|Proteomes:UP000017904}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:274 {ECO:0000313|Proteomes:UP000017904};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC       {ECO:0000256|ARBA:ARBA00008668}.
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:CDC19426.1}.
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DR   EMBL; CBEX010000042; CDC19426.1; -; Genomic_DNA.
DR   STRING; 1262888.BN582_00245; -.
DR   Proteomes; UP000017904; Unassembled WGS sequence.
DR   GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030599; F:pectinesterase activity; IEA:InterPro.
DR   GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR   CDD; cd01821; Rhamnogalacturan_acetylesterase_like; 1.
DR   Gene3D; 2.60.40.1080; -; 1.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 2.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR   InterPro; IPR003343; Big_2.
DR   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR033131; Pectinesterase_Asp_AS.
DR   InterPro; IPR000070; Pectinesterase_cat.
DR   InterPro; IPR037459; RhgT-like.
DR   InterPro; IPR013830; SGNH_hydro.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   InterPro; IPR001119; SLH_dom.
DR   PANTHER; PTHR43695; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G17250)-RELATED; 1.
DR   PANTHER; PTHR43695:SF1; RHAMNOGALACTURONAN ACETYLESTERASE; 1.
DR   Pfam; PF02368; Big_2; 1.
DR   Pfam; PF13472; Lipase_GDSL_2; 1.
DR   Pfam; PF01095; Pectinesterase; 1.
DR   Pfam; PF00395; SLH; 1.
DR   SMART; SM00635; BID_2; 1.
DR   SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   SUPFAM; SSF52266; SGNH hydrolase; 2.
DR   PROSITE; PS00503; PECTINESTERASE_2; 1.
DR   PROSITE; PS51272; SLH; 1.
PE   3: Inferred from homology;
KW   Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017904};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..1393
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004415758"
FT   DOMAIN          1302..1365
FT                   /note="SLH"
FT                   /evidence="ECO:0000259|PROSITE:PS51272"
FT   ACT_SITE        208
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ   SEQUENCE   1393 AA;  152889 MW;  BC6E0E08AE0219CD CRC64;
     MKISIKKLFS SILAVTMVCG LLPTGTIVMA QATTITVGKG SGYDFSTVQS AIDSIKIIPT
     EKDPVTIEIA SGTYEESVSV NKPNVHITHD GKPEEVVITY DKANGHSNPA KNFGTDNTST
     FSLGVNATGF KADNITVQNS YNIGTNNSQV QAVAFSSQAD KVVLNNCRLI GRQDTLYLRG
     ASKGQTNYGS ANSVRTYLKN CYIEGTVDYI FGDGTAFFDK CNLKMMAYQN GGHFTAPNTT
     LFNIGYVFNE CNLSVDKTAT ADILGKIDLG RPWQCDGAYP SYGSNSVFIN CTLPDNINKA
     GFSKWDENTV LNKVRFYEYN SKDSKGRTLD TKNRAEFVKE LTEKQAKQYN CYNVLKGEDG
     WNPALASGTT DVCDITLNGY NLSIPVDETY TLKAFTLPVK AKTKVTYNSS DENIASVDNN
     GVVKAKVVGE CKITATTETG MSATANVTVT AERTALPTLK SVSIEKDSSI KVGQKLKAVY
     SYNLDTDNEA DAANIRWYAV DGSKKILIKE GVGEYFQSYE VEAKDVGYNI MVEVMPATKT
     TYGEYGATGT YTTKAKVTGN SSTPNTLYRS NFDSINGWTT KNKWNIFSNG YNNFVTAGCE
     NGNTCLMTFD KGTNWNNVNI DGRFRFNPDG KGLTSEGFFN IYMNYNTNSY YKLTLGRGSN
     TKSVKLYIYK NDGTGEVLLG KDETSLKNNI YQNSGEDNPY FYVTFAKTGD NLTAKVRFEG
     QTKPTAILTA KETGNALSAG TVAMEAGGDA NIVLVDSLSV ESAEEEDDSN KTRIFILGDS
     TVKYYGDDNT IGGWGEYLVN YFNADSVKFI NKAEGGRSTR SFINQGRLAE AMSEVRKGDY
     VFIQFGTNDQ RTDANAFMEH SVALGTPDTN GIYPTVPGVK SKTPDSIYNF YKDTDYPYAE
     TFYSYNTGTF KWYLDQYVTA VRQAGGVPVL LTPACRIFFD SNGKITSHFG ENDGYVTAVR
     QVAEEQKVEL IDMFNITKDL YESYGVFTTQ GLHNIKEDGT VDLTHYNKFG ANLIAGKMAD
     AIKSLNLSGV SENVIASNKE VAKTDSLKSA NLVIVGGKGA AGDNEGDYRV DAAGFGNYIS
     NYLSDKITVK NLAQTDATAK SFSRSDKYNE FLNSFKEGDY VMIAFTNEDK YTSDDIKYYS
     SPYGNVDTTG SYEQFLYYSY VKPVLDKKAI PILVTPYYER TEENGELTAT ENPYVNAVKD
     LVVSKQLFFV NMYDLSKNLY DVMGAEGSKV LNAYDAKGKI CGDTFSTFGA ETMAKKILTA
     LKQSSASLKD YINDTKLTAV SYMTRADFTY MVIDALGCEI NNGNSFADVS KGKYYQGAIA
     TAKNLGLVTA VDGNNFHPEE PVTADFLQSV IDKALKHKKS NADFKDVYAL AKGKVSNEIG
     IYAIDKLNEE INK
//
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