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Database: UniProt/TrEMBL
Entry: Q4V1B2_BACCZ
LinkDB: Q4V1B2_BACCZ
Original site: Q4V1B2_BACCZ 
ID   Q4V1B2_BACCZ            Unreviewed;       791 AA.
AC   Q4V1B2;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   01-MAY-2013, entry version 38.
DE   SubName: Full=Pyruvated mannose-specific xanthan lyase;
DE            EC=4.2.2.12;
GN   Name=xalA; OrderedLocusNames=pE33L466_0352;
OS   Bacillus cereus (strain ZK / E33L).
OG   Plasmid pE33L466.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=288681;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZK / E33L;
RX   PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S.,
RA   Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O.,
RA   Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T.,
RA   Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA   Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA   Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA   Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G.,
RA   Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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DR   EMBL; CP000040; AAY60495.1; -; Genomic_DNA.
DR   RefSeq; YP_245833.1; NC_007103.1.
DR   ProteinModelPortal; Q4V1B2; -.
DR   STRING; 288681.pE33L466_0352; -.
DR   CAZy; PL8; Polysaccharide Lyase Family 8.
DR   EnsemblBacteria; AAY60495; AAY60495; pE33L466_0352.
DR   GeneID; 3399921; -.
DR   KEGG; bcz:pE33L466_0352; -.
DR   eggNOG; NOG04835; -.
DR   HOGENOM; HOG000136478; -.
DR   ProtClustDB; CLSK2525442; -.
DR   BioCyc; BCER288681:GHG7-422-MONOMER; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0047492; F:xanthan lyase activity; IEA:EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.100; -; 1.
DR   Gene3D; 2.60.220.10; -; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   InterPro; IPR008929; Chondroitin_lyas.
DR   InterPro; IPR011013; Gal_mutarotase_SF_dom.
DR   InterPro; IPR014718; Glyco_hydro-type_carb-bd_sub.
DR   InterPro; IPR011071; Lyase_8-like_C.
DR   InterPro; IPR012970; Lyase_8_alpha_N.
DR   InterPro; IPR004103; Lyase_8_C.
DR   InterPro; IPR003159; Lyase_8_central_dom.
DR   InterPro; IPR012329; Lyase_8_N.
DR   Pfam; PF02278; Lyase_8; 1.
DR   Pfam; PF02884; Lyase_8_C; 1.
DR   Pfam; PF08124; Lyase_8_N; 1.
DR   SUPFAM; SSF48230; Chondroitin_lyas; 1.
DR   SUPFAM; SSF74650; Gal_mut_like; 1.
DR   SUPFAM; SSF49863; Lyase_like_C; 1.
PE   4: Predicted;
KW   Complete proteome; Lyase; Plasmid; Pyruvate.
SQ   SEQUENCE   791 AA;  89695 MW;  F1CEFB542E8308AB CRC64;
     MIKENGFMKR IILCIFVLSF VMGSFSLNAV AETEESAKMI SNWKRVLVGE PFTNDDVILK
     NIVWDKEKDL QDNVLSNLNK ENESPSLFKN LPDWKQNSAQ ITETVKNIEK MAVLYQTPNS
     IYYQKDTLQK DIMYAIEYFY DQMYNEKIKN TYGNWWDWEI GIPQSYNNIL VLMFDDLTEV
     ELSKYIMAVD RFVPDPTKRL NGIKETGANL LDKSFIVMVR GILNNNNNKI QLGIDATNDV
     YKIVQNGDGF YKDGSFIQHT YNPYTGGYGE VLLARSADIH ELFSGTDRLT NVQGIKKLYT
     YIETTYLPVM KQGEVFDMTR GRGMSRQNSS SSIVGRNILY EILVISSQNQ DLSYRGKYAR
     YVKEAIFQHN DSESYYNGLS IHKTQTFQRL MSDSSIKPDF GVRDTNNMLS AMNQMTHQKK
     DFAAGLSLFG KQISSFEYGN GENMKGFYMG TGMLYLYNND LGQYDNDYWA TIDMTRLPGT
     TTDHKLGNLI DWKNYNNPKS WSGGVSDGQI GSASMYYTMQ NVTGSSLEAK KSWFFLKDKI
     VAMAAGINSK ENADTETIVE NRRLGKNGSN LLKVENTEVA LDQGILFKGA SWAHLKGKNN
     QSDIGYVFPQ SENIYAEKKE RSGKWSDVNK GGSSDQVSNM FATLSIPHGK SPSGGEYVYV
     ILPGKNQEET STYAKEMDVS ILSNTPMQQV IYDDADDIWM GNFYEIGKVN EVEAKTRGTI
     AINYKGNGVK VVMADPMKEQ AKVIFTIPKK LGYKVAEKDD EITVKEDANS WIIEMDSSDK
     SGKSSQVYFE Q
//
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