ID B0C573_ACAM1 Unreviewed; 663 AA.
AC B0C573;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Heparin-sulfate lyase N-terminal domain-containing protein {ECO:0000259|Pfam:PF16889};
GN OrderedLocusNames=AM1_1276 {ECO:0000313|EMBL:ABW26313.1};
OS Acaryochloris marina (strain MBIC 11017).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC Acaryochloridaceae; Acaryochloris.
OX NCBI_TaxID=329726 {ECO:0000313|EMBL:ABW26313.1, ECO:0000313|Proteomes:UP000000268};
RN [1] {ECO:0000313|EMBL:ABW26313.1, ECO:0000313|Proteomes:UP000000268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBIC 11017 {ECO:0000313|Proteomes:UP000000268};
RX PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA Blankenship R.E., Touchman J.W.;
RT "Niche adaptation and genome expansion in the chlorophyll d-producing
RT cyanobacterium Acaryochloris marina.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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DR EMBL; CP000828; ABW26313.1; -; Genomic_DNA.
DR AlphaFoldDB; B0C573; -.
DR CAZy; PL12; Polysaccharide Lyase Family 12.
DR KEGG; amr:AM1_1276; -.
DR eggNOG; COG5360; Bacteria.
DR HOGENOM; CLU_013047_1_0_3; -.
DR Proteomes; UP000000268; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000000268};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 18..343
FT /note="Heparin-sulfate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16889"
SQ SEQUENCE 663 AA; 76827 MW; 91BA0D7C5DBA9B61 CRC64;
MKSVDELCQK HPKLITNLFE NINIEHPGLE TVREYVNKGD YTQASHSLIT YFRNKPDKIG
WKNLLPEQKF NKDLDADHIL NNEFIFQRIS GTVPQDNDRF NWSYLGTKED SEWAWFLNRH
YHVVDLFHAY LRSGNSDYVQ YIYLSIRDWI LTSIAAPNTH YWAQWRGREV ACRILHWAPI
FYGLLESPNF SDVDHLLMLA ILPVHGNFLR HCHTWGANWL AREMNGLATL AICWPEFKFS
QSWLTYAQFH MSREIELQVY PDGSHKELTS HYHRVTLLDF DNFAKLMQLS GHNLSISFGK
TLERMWNYLA FAMRPDGSSP LNNDSDRDEL RTTIKSVANL YNRSDWQYIA SNGQEGDGPL
SPSILFPWAG QVIMRSSWNK DAHWAFFDVG PHGINYHTHN DKLHLSVAAF GRDLLVDSGR
YHYKRDSFWH YFRNSASHNT ILVDGQGQNA GIGEALNPVE QQFYSTPEFD FAYGKFDQGY
QGVADKVIHS RFLVYLRHQY WVVIDRVSAS NAHQIQTLWH FHPDCNLEVQ GSSIVTTNEN
CGNLRIVPTD NLSWDIDIAR GSMEPIQGWW SKEYNHKQPN PTAIYSSHLS TTATFAWILC
PARGVVPPID VQYQSISDDQ IELEITHTSN RIQLSLYLNE QHILHSLSSH PEAIIQVKGL
KPE
//
