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Database: UniProt
Entry: A0A1V3MSF2_9SPHI
LinkDB: A0A1V3MSF2_9SPHI
Original site: A0A1V3MSF2_9SPHI 
ID   A0A1V3MSF2_9SPHI        Unreviewed;       609 AA.
AC   A0A1V3MSF2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Heparinase {ECO:0000313|EMBL:OOG15720.1};
GN   ORFNames=BWD42_23860 {ECO:0000313|EMBL:OOG15720.1};
OS   Sphingobacterium sp. CZ-UAM.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=1933868 {ECO:0000313|EMBL:OOG15720.1, ECO:0000313|Proteomes:UP000188865};
RN   [1] {ECO:0000313|EMBL:OOG15720.1, ECO:0000313|Proteomes:UP000188865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CZ-UAM {ECO:0000313|EMBL:OOG15720.1,
RC   ECO:0000313|Proteomes:UP000188865};
RA   Steffani-Vallejo J.L., Licona-Cassani C., Cruz-Morales P., Lozano L.,
RA   Zuniga C., Morales M., Revah S., Utrilla J.;
RT   "Genome sequence of Sphingobacterium sp. CZ-UAM, isolated from a
RT   methanotrophic consortium.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:OOG15720.1}.
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DR   EMBL; MTCM01000011; OOG15720.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V3MSF2; -.
DR   STRING; 1933868.BWD42_23860; -.
DR   OrthoDB; 7335480at2; -.
DR   Proteomes; UP000188865; 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; IPR008929; Chondroitin_lyas.
DR   InterPro; IPR012480; Hepar_II_III.
DR   InterPro; IPR031680; Hepar_II_III_N.
DR   PANTHER; PTHR39210; HEPARIN-SULFATE LYASE; 1.
DR   PANTHER; PTHR39210:SF1; HEPARIN-SULFATE LYASE; 1.
DR   Pfam; PF07940; Hepar_II_III; 1.
DR   Pfam; PF16889; Hepar_II_III_N; 1.
DR   SUPFAM; SSF48230; Chondroitin AC/alginate lyase; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          87..327
FT                   /note="Heparin-sulfate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16889"
SQ   SEQUENCE   609 AA;  72594 MW;  027FB3530C9EA157 CRC64;
     MGTRYTIYRI RHELEKKIGY LKKKHPVNLS FKVPITISDW KASHNPYVIE PKEALLIPKE
     HFEPLREKAE RILAGEIQFF SSEWRSLGKD YNWITNPSTG YQYDITTHWS QIPDISEDAG
     DIKFVWEKSR FSYLLTLIRY DYHFDKDLSE FIFSEIEDWI DSNPINQGPN WRCSQEISLR
     ILNWCFAIYY YQNSDALTEE RWQKIQNVVY ASIHHVYHHI DFSRIAVRNN HAITETLFLT
     LSNILFPFIP ETKDWSKKGL KWFEDEINYQ IYDDGTFLQF SMNYHRVVIQ LLSLGISVFH
     KNNRNFPKFI YNKAYRSLNF LYQCMQDENG KLPNYGSNDG ALFFPLADAD YRDYRPQLNT
     LHYILTNKAL FEEREILEDL NWNGKISCIN VFPPLRKQQG VQSFDIGGYF VCRDNGFFTF
     IRCGDHKDRP AQADNLHLDI WYQGKNILRD SGTYKYNTDS EKLRYFMGSL SHNVVVVNEE
     SQMLKGGRFI WYYWTQKLHA GWSETNNDYI FSGEIKAFQF LNKNATHRRK IYISKKSLNW
     IIEDELRNLE NYKMKQVWHP ADPRLKIEAE CAKSEFSSYN SDYYGSYTKE KSIFFEFHNK
     ISSIITFNI
//
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