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
//