GenomeNet

Database: UniProt/TrEMBL
Entry: A0A0K1U894_9ALTE
LinkDB: A0A0K1U894_9ALTE
Original site: A0A0K1U894_9ALTE 
ID   A0A0K1U894_9ALTE        Unreviewed;       558 AA.
AC   A0A0K1U894;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   07-JUN-2017, entry version 8.
DE   SubName: Full=Glutamate decarboxylase {ECO:0000313|EMBL:AKV95966.1};
GN   ORFNames=ACP86_07250 {ECO:0000313|EMBL:AKV95966.1};
OS   Marinobacter sp. CP1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Marinobacter.
OX   NCBI_TaxID=1671721 {ECO:0000313|EMBL:AKV95966.1};
RN   [1] {ECO:0000313|EMBL:AKV95966.1, ECO:0000313|Proteomes:UP000057932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CP1 {ECO:0000313|EMBL:AKV95966.1,
RC   ECO:0000313|Proteomes:UP000057932};
RX   PubMed=26404584;
RA   Wang Z., Eddie B.J., Malanoski A.P., Hervey W.J.IV., Lin B.,
RA   Strycharz-Glaven S.M.;
RT   "Complete Genome Sequence of Marinobacter sp. CP1, Isolated from a
RT   Self-Regenerating Biocathode Biofilm.";
RL   Genome Announc. 3:e01103-15(2015).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP011929; AKV95966.1; -; Genomic_DNA.
DR   RefSeq; WP_008173510.1; NZ_CP011929.1.
DR   EnsemblBacteria; AKV95966; AKV95966; ACP86_07250.
DR   KEGG; mari:ACP86_07250; -.
DR   PATRIC; fig|1671721.3.peg.1500; -.
DR   KO; K01580; -.
DR   Proteomes; UP000057932; Chromosome.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR022517; Asp_decarboxylase_pyridox.
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   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03799; NOD_PanD_pyr; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000057932};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES     338    338       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   558 AA;  62389 MW;  D0B33DFA4D6A1583 CRC64;
     MTGKKKSAQA SVEAMYRVFT VPEAPESTLS RIDQNISRNL AGFLQEHIVA VERDLSDVEK
     DFSDYSIPEK PVFVSEQAQF LLDKLVANSV HTASPAFIGH MTSALPYFML PLSKIMIALN
     QNLVKTETSK AFTPMERQVL GMIHRLVYQE DGAFYRKWMH DPRYALGAMC SGGTVANLTA
     LWVARNRAFP AEGSFRGLHQ EGLFRALKYY GYEGAAIVVS RRGHYSLRKA ADVLGLGRES
     LIPVDTDDEN RINTDALRDK CLELQRQKIK VMAICGVAGT TETGNVDPLD AMADIAREFG
     AHFHVDAAWG GPTLFSRTYK HLLRGIEKAD SVTFDAHKQL YVPMGVGLVV FRDPSLASAV
     EHHAQYIIRK GSRDLGSTTL EGSRPGMSML IHSGLKILAR EGYEILIDQG IDKAKTFAEM
     IEAEPDFELV TRPELNILTY RYCPENVQEA LACADPLQAE KLNTCLNRIT KFIQKTQRER
     GKAFVSRTRL EPARYYNFPC IVFRVVLANP LTTKEILADI LSEQRELSRD EGIEDEISIL
     HQMADAVLKQ ATPNARQA
//
DBGET integrated database retrieval system