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Database: UniProt/TrEMBL
Entry: A0A085UBP8_YERRU
LinkDB: A0A085UBP8_YERRU
Original site: A0A085UBP8_YERRU 
ID   A0A085UBP8_YERRU        Unreviewed;       467 AA.
AC   A0A085UBP8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   25-OCT-2017, entry version 26.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=CSF007_10490 {ECO:0000313|EMBL:CEK27848.1}, nADLYRO1b_35
GN   {ECO:0000313|EMBL:KFE40611.1};
OS   Yersinia ruckeri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=29486 {ECO:0000313|EMBL:KFE40611.1, ECO:0000313|Proteomes:UP000054283};
RN   [1] {ECO:0000313|EMBL:KFE40611.1, ECO:0000313|Proteomes:UP000054283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=37551 {ECO:0000313|EMBL:KFE40611.1,
RC   ECO:0000313|Proteomes:UP000054283};
RA   Navas E., Bohle H., Henriquez P., Grothusen H., Bustamante F.,
RA   Bustos P., Mancilla M.;
RT   "Draft genome sequence of the fish pathogen Yersinia ruckeri (37551)
RT   serotype O1b, isolated from diseased, vaccinated Atlantic salmon
RT   (Salmo salar) in Chile.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CEK27848.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CSF007-82 {ECO:0000313|EMBL:CEK27848.1};
RA   Colston Sophie, Beka Lidia, Wegrzyn Jill, Nelson C.Michael.,
RA   Graf Joerg;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:CEK27848.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CSF007-82 {ECO:0000313|EMBL:CEK27848.1};
RA   Nelson M.C., LaPatra S.E., Welch T.J., Graf J.;
RT   "Complete Genome Sequence of Yersinia ruckeri Strain CSF007-82,
RT   Etiologic Agent of Red Mouth Disease in Salmonid Fish.";
RL   Genome Announc. 3:1-2(2015).
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC       {ECO:0000256|RuleBase:RU361171}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         ECO:0000256|RuleBase:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; LN681231; CEK27848.1; -; Genomic_DNA.
DR   EMBL; JPFO01000001; KFE40611.1; -; Genomic_DNA.
DR   RefSeq; WP_004721801.1; NZ_MKFJ01000012.1.
DR   EnsemblBacteria; KFE40611; KFE40611; nADLYRO1b_35.
DR   GeneID; 29467066; -.
DR   KEGG; yrb:UGYR_03340; -.
DR   PATRIC; fig|29486.44.peg.37; -.
DR   KO; K01580; -.
DR   Proteomes; UP000054283; Unassembled WGS sequence.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006536; P:glutamate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR010107; Glutamate_decarboxylase.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   InterPro; IPR021115; Pyridoxal-P_BS.
DR   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000054283};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171, ECO:0000313|EMBL:KFE40611.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054283}.
FT   MOD_RES     277    277       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   467 AA;  52710 MW;  C77EA4C560560191 CRC64;
     MTKKNDTNDF RSTLLDSRFG SESIRHIAES KRFPEKEIRE DVAFQIINDE LFLDGNARQN
     LATFCQTWDD DNVHKLMDLS INKNWIDKEE YPQSAAIDMR CVNMVADLWN APKQKNGQAV
     GTNTIGSSEA CMLGGMAMKW RWRKRMEAAG KPTNKPNFVC GPVQVCWHKF ARYWDVEIRE
     LPMEPGQLFM DPQRMIEACD ENTIGVVPTF GVTYTGNYEF PKPLHDALDK LQRETGLDID
     MHIDAASGGF LAPFVAPDIE WDFRLPRVKS ISTSGHKFGL APLGCGWVIW RDEASLPEEL
     VFKVDYLGGQ VGTFAINFSR PAGQVIAQYY EFLRLGREGY TKVQSASYQV AAFLAEEIAK
     LGSYEFICSG GVEEGIPAVC FRVKEGAKPG YTLYDLSERL RLRGWQVPAF ALNGGMSDVV
     VMRIMCRRGF EMDFAELLLE DFKSSLNYLS QHPSLGGLAS QNSFKHT
//
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