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Database: UniProt
Entry: C2LIS2_PROMI
LinkDB: C2LIS2_PROMI
Original site: C2LIS2_PROMI 
ID   C2LIS2_PROMI            Unreviewed;      1021 AA.
AC   C2LIS2;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   16-OCT-2013, entry version 16.
DE   RecName: Full=Chondroitin sulfate ABC lyase;
DE   AltName: Full=Chondroitin ABC eliminase;
DE   AltName: Full=Chondroitin ABC lyase;
DE   AltName: Full=Chondroitinase ABC;
GN   ORFNames=HMPREF0693_1762;
OS   Proteus mirabilis ATCC 29906.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Proteus.
OX   NCBI_TaxID=525369;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 29906;
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C.,
RA   Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L.,
RA   Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y.,
RA   Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L.,
RA   Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F.,
RA   Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M.,
RA   Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S.,
RA   Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J.,
RA   Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J.,
RA   Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D.,
RA   Worley K., Gibbs R.;
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Broad-specificity glycosaminoglycan lyase (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data.
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DR   EMBL; ACLE01000033; EEI48514.1; -; Genomic_DNA.
DR   EnsemblBacteria; EEI48514; EEI48514; HMPREF0693_1762.
DR   PATRIC; 36134048; VBIProMir92659_1030.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016837; F:carbon-oxygen lyase activity, acting on polysaccharides; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.50.10.100; -; 1.
DR   Gene3D; 2.60.120.410; -; 1.
DR   Gene3D; 2.60.220.10; -; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   InterPro; IPR008929; Chondroitin_lyas.
DR   InterPro; IPR024200; Chondroitinase_ABC_I.
DR   InterPro; IPR011013; Gal_mutarotase_SF_dom.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR014718; Glyco_hydro-type_carb-bd_sub.
DR   InterPro; IPR011071; Lyase_8-like_C.
DR   InterPro; IPR004103; Lyase_8_C.
DR   InterPro; IPR003159; Lyase_8_central_dom.
DR   InterPro; IPR012329; Lyase_8_N.
DR   InterPro; IPR015177; Lyase_catalyt.
DR   InterPro; IPR015176; Lyase_N.
DR   Pfam; PF02278; Lyase_8; 1.
DR   Pfam; PF02884; Lyase_8_C; 1.
DR   Pfam; PF09093; Lyase_catalyt; 1.
DR   Pfam; PF09092; Lyase_N; 1.
DR   PIRSF; PIRSF034515; Chondroitinase; 1.
DR   SUPFAM; SSF48230; SSF48230; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF49863; SSF49863; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Lyase.
SQ   SEQUENCE   1021 AA;  115116 MW;  2EA5DD67A403681B CRC64;
     MPIFRFTALA MTLGLLSTPY HVIAATSNPA FDPNHLMQSE IYHFAQSDPL ADFSSDKNST
     LTLSDKRSIM GNQSLLWQWK GGSSFTLHKK LIVPTDKEAS KAWGRASTPV LSFWLYNEKP
     IDGYLTVDLG EKLNATSEAQ AGFKVKLNFT GWRAIGISLN NDLENREMTL NATNTSSDGT
     QDSIGRSLGA NVDSIRFKAP SNISQGEIYI DRIMFSIDDA RYQWSDYQIK TRLSEPEIEF
     HTVQPQLPVT PENLAAIDLI RQRLINEFVG GEKETNLALE ENISKLKTDF EALNIRPLSD
     GGMQGRHLIT DKQTIIYQPE QLNSQDKQLF DNYVILGNYT TLMFNISRAY VLEKDPTQKE
     QLKQMYLLMT KHLLDQGFVK GSALVTTHHW GYSSRWWYIS TLLMADALKE ANLQTEVYDS
     LLWYSREFKS SFDMKVGANS SDLDYFNTLS RQHLALLLLE PDDQKRINLV NSFNHYITGA
     LTQVPPGSKD GLRPDGTAWR HEGNYPGYSF PAFKNASQLI YLLRETPFAV GESGWNNLKK
     AMISAWIYSN PEVGLPLAGR HPFNSPSLQS IAQGYYWLAM SAQPAPDKQL ASIYLAISGK
     SRNESPTIFG EEITPASLPQ GFYAFNGGAF GIHRWQDKMV TLKAYNTNVW SSEIYNKDNR
     YGRYQSHGVA QIVRNGSQLS QGYQQEGWDW NRMPGATTIH LPLKELDSPN PHTLMQRGER
     GFSGTSALEG KYGMMAFDLL YPANLARFDA NFTAKKTVLA ADNHLIFVGS NINSSDKDHP
     VETTLFQHAI TPELNTIWIN GQKIEGFPYQ TTLKQGDWII DSNGNGYLIT QAEKVNVSRQ
     HQTSAENKNR QPTQGNFSSA WIDHGIQPKD HSYEYMVFLD ATPEKMAQLA EKFRANNGLY
     QVIRKDKDVH IIYDKLSQIT GYAFYQPAVI DDKWIKKVDK PSIVMTHQEG NILTVSAVTP
     DLNMTRQKAA TPVTINVTVK GKWQPTAQDS EVKYNVSGDN TELIFTSYFG IPQEIKLSPL
     S
//
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