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Database: UniProt/TrEMBL
Entry: A1U6N4_MARHV
LinkDB: A1U6N4_MARHV
Original site: A1U6N4_MARHV 
ID   A1U6N4_MARHV            Unreviewed;       611 AA.
AC   A1U6N4;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   25-OCT-2017, entry version 69.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ABM20653.1};
GN   OrderedLocusNames=Maqu_3584 {ECO:0000313|EMBL:ABM20653.1};
OS   Marinobacter hydrocarbonoclasticus (strain ATCC 700491 / DSM 11845 /
OS   VT8).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Marinobacter.
OX   NCBI_TaxID=351348 {ECO:0000313|EMBL:ABM20653.1, ECO:0000313|Proteomes:UP000000998};
RN   [1] {ECO:0000313|Proteomes:UP000000998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700491 / DSM 11845 / VT8
RC   {ECO:0000313|Proteomes:UP000000998};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Edwards K., Richardson P.;
RT   "Complete sequence of chromosome 1 of Marinobacter aquaeolei VT8.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50};
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DR   EMBL; CP000514; ABM20653.1; -; Genomic_DNA.
DR   ProteinModelPortal; A1U6N4; -.
DR   STRING; 351348.Maqu_3584; -.
DR   EnsemblBacteria; ABM20653; ABM20653; Maqu_3584.
DR   KEGG; maq:Maqu_3584; -.
DR   eggNOG; ENOG4105DY8; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000282553; -.
DR   KO; K01580; -.
DR   OMA; TVNPHKM; -.
DR   OrthoDB; POG091H05DC; -.
DR   Proteomes; UP000000998; 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   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000998};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50}.
FT   MOD_RES     391    391       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   611 AA;  68161 MW;  A454E02506D6E520 CRC64;
     MASLPDRSYT TQPQGTNAPL GGWQTFFATG PRPAPSDGFP EPTHRIPLNV CGAMTGKKKS
     AQASLEAMYR VFTVPEAPES TLSRIDQDIS RNLAGFLQEH IVAIERDLSE VEKDFSDYVI
     PEKPVFVSEQ TQFLLDKLVA NSVHTASPAF IGHMTSALPY FMLPLSKIMI ALNQNLVKTE
     TSKAFTPMER QVLGQIHRLV YQEDGSFYRK WMHDPRHALG AMCSGGTVAN LTALWVARNR
     AFPAEGSFRG LHEEGLFRAL KYYGHEGAAI VVSKRGHYSL RKAADVLGLG RDALVPVETD
     EFNRIQTDAL RDKCLELQKQ KIKIMAICGV AGTTETGNVD PLDAMADIAR EFGAHFHVDA
     AWGGPTLFSR THRHLLRGIE KADSVTFDAH KQLYVPMGAG LVVFKDPSLA SAVEHHAQYI
     IRKGSRDLGS TTLEGSRPGM AMLIHSGLKI LAREGYEILI DQGIDKAKTF ANMIDEQPDF
     ELVTRPELNI LTYRYCPEDV RQALAMADEL QAEKMNTCLN RITKFIQKTQ RERGKAFVSR
     TRLEPARYYH FPCIVFRVVL ANPLTTPDIL EDILREQREL SKEDGIADEM AILHQMAAAV
     LKQNQKEARQ A
//
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