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Database: UniProt
Entry: A0A1F3LGE8_9BACT
LinkDB: A0A1F3LGE8_9BACT
Original site: A0A1F3LGE8_9BACT 
ID   A0A1F3LGE8_9BACT        Unreviewed;       738 AA.
AC   A0A1F3LGE8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Chondroitin lyase {ECO:0000313|EMBL:OFY39710.1};
GN   ORFNames=A2X18_09890 {ECO:0000313|EMBL:OFY39710.1};
OS   Bacteroidetes bacterium GWF2_40_14.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1797347 {ECO:0000313|EMBL:OFY39710.1, ECO:0000313|Proteomes:UP000176561};
RN   [1] {ECO:0000313|EMBL:OFY39710.1, ECO:0000313|Proteomes:UP000176561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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:OFY39710.1}.
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DR   EMBL; MEOK01000029; OFY39710.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F3LGE8; -.
DR   STRING; 1797347.A2X18_09890; -.
DR   Proteomes; UP000176561; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.70.98.70; -; 1.
DR   Gene3D; 1.50.10.100; Chondroitin AC/alginate lyase; 1.
DR   InterPro; IPR008397; Alginate_lyase_dom.
DR   InterPro; IPR008929; Chondroitin_lyas.
DR   InterPro; IPR012480; Hepar_II_III.
DR   PANTHER; PTHR39210; HEPARIN-SULFATE LYASE; 1.
DR   PANTHER; PTHR39210:SF1; HEPARIN-SULFATE LYASE; 1.
DR   Pfam; PF05426; Alginate_lyase; 1.
DR   Pfam; PF07940; Hepar_II_III; 1.
DR   SUPFAM; SSF48230; Chondroitin AC/alginate lyase; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:OFY39710.1};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          104..325
FT                   /note="Alginate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF05426"
SQ   SEQUENCE   738 AA;  83695 MW;  4CEEE1B8A417671A CRC64;
     MPQNLITDLQ NQVNYLLKTS ESDKMKKPLI IITLLIFANV IIAREHPSLM MTGKGVAEMK
     KGMGKYPAFD ASIEETKTKA DFAIASPIVV PVPKDGGGGA THEKHKDNYY SMYYCGIMFQ
     LTGEKKYAGF VEKMLDEYLK LYPTLGYHPV KMSSNPGRLF WQTLNDFVWL VHTSIAYDCV
     YNYLPEQKRT EYNNKLFKPM AQFLMDGSDA NNKIFNKMHN HGTWACAAVG MIGYVMDDNE
     LIQKALYGSD KTGKNGGYMQ QLDELFSPDG YFTEGAYYQR YAIWPFVIFA QAINNNDPDK
     KIFLYRDAIL KKAVSTLIQM TYNGEFFTIN DALKKGFSAQ ELVFADNILY AADNSQKELL
     TISKNYQSFF LPSDAGFAVA RDIARGEAKE FKLISQLLRD GSDGKMGGLA IFRSPKPAEN
     TTFLMKATSH GLSHGHFDKL TISYYDDGNP ILVDYGSSRF LNIVVKYNGG YTPLNDKYSM
     STISHNTVSV DMKSHYEGDI KVSSNYAPTI YCYDISNPEI QVCSAYETNA SPGVKMQRTN
     AVIENLGGVR IILDIFKLTS EKEHTYDLPF FYNGDMISLS TPYTKALEQM GIFGNSDGYR
     YLWKEAWAKP NDSKVCFTWL KGRRFYSVTT VTDSKSDLFF VRSGANDPEY YLRTDPAFII
     RQNSAKNHTF LSAIETHGKY DLVVEKTENA VSSVKSLRII EDNDNYTVAE IEVNEVKARF
     RIDYNKESSA AKWTFNKY
//
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