ID B9Y533_9FIRM Unreviewed; 675 AA.
AC B9Y533;
DT 14-APR-2009, integrated into UniProtKB/TrEMBL.
DT 14-APR-2009, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Heparinase II/III-like protein {ECO:0000313|EMBL:EEF68946.1};
GN ORFNames=HOLDEFILI_00914 {ECO:0000313|EMBL:EEF68946.1};
OS Holdemania filiformis DSM 12042.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Holdemania.
OX NCBI_TaxID=545696 {ECO:0000313|EMBL:EEF68946.1, ECO:0000313|Proteomes:UP000005950};
RN [1] {ECO:0000313|EMBL:EEF68946.1, ECO:0000313|Proteomes:UP000005950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12042 {ECO:0000313|EMBL:EEF68946.1,
RC ECO:0000313|Proteomes:UP000005950};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEF68946.1, ECO:0000313|Proteomes:UP000005950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12042 {ECO:0000313|EMBL:EEF68946.1,
RC ECO:0000313|Proteomes:UP000005950};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Holdemania filiformis DSM 12042.";
RL Submitted (FEB-2009) 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:EEF68946.1}.
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DR EMBL; ACCF01000054; EEF68946.1; -; Genomic_DNA.
DR RefSeq; WP_006058124.1; NZ_GG657553.1.
DR AlphaFoldDB; B9Y533; -.
DR STRING; 545696.HOLDEFILI_00914; -.
DR eggNOG; COG5434; Bacteria.
DR HOGENOM; CLU_013047_0_0_9; -.
DR OrthoDB; 7335480at2; -.
DR Proteomes; UP000005950; 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 39..303
FT /note="Heparin-sulfate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16889"
SQ SEQUENCE 675 AA; 76970 MW; 4BB4A12CAC943934 CRC64;
MKKNEFFAQK KQFFVNDVAA VKDYVLTHCA QDQIDKIIAR ADEACAQSFR FDLRWDMEYT
EIPVVFEKEI NWLHQPADDP EWIFAFNRHH FWITMGQAYV LTGDEKYAEA FVKQCKSWIC
QINLRDPDCA NACRTLETGI RMNLWIKAFC LFRNSPALTD GFCSLFEESI LEQEKFIAEV
WNSTKIISNW GVLENHGLFT AALLMPEHPF SEEMRKEALR RLDLQLQRQV YPDGVHWEQS
TMYHNEVAQD FLEVKILADR NGIALPSGYN ERLAKMIDFC VEHRKPDGNE MAMGDSDDID
VRDIITKAAV SFNNPAWKAA GYREFDFDCV FDLGAEAATA YASMPSLPSG KRSVIFPDSG
HIFWHSDDSA DQTWLHFTNG VHGGGHAHED KLHVDLFYRG EDIVRDSGRL TYVDKPERYE
FKGPKAHNVI ELDDQPSIRC KRSWGYHKRS WSLNTQMSEA GSFRLAQGAA LGYMDLETGS
AVLSRKVVWL REDLILVHDE IYANPKDKHK IVQRWHFSPD AQVMLKGQTA GLTLNNSDCE
VLTLAEQAEV RLTETRLSLH YNTTTPSVML ETELNEAGFT SITTIFSLNP KGEKAPCFAV
PAPVSLVSRQ DRPFAKSVAE GWVIQKGADQ FTVMIAHEDY MGPSDAVLVN ERQGMGHVIV
WSGLDKEQWG TTLAY
//
