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Database: UniProt/TrEMBL
Entry: Q487K9_COLP3
LinkDB: Q487K9_COLP3
Original site: Q487K9_COLP3 
ID   Q487K9_COLP3            Unreviewed;       543 AA.
AC   Q487K9;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   28-MAR-2018, entry version 79.
DE   SubName: Full=Putative decarboxylase {ECO:0000313|EMBL:AAZ25150.1};
GN   OrderedLocusNames=CPS_1007 {ECO:0000313|EMBL:AAZ25150.1};
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879 {ECO:0000313|EMBL:AAZ25150.1, ECO:0000313|Proteomes:UP000000547};
RN   [1] {ECO:0000313|EMBL:AAZ25150.1, ECO:0000313|Proteomes:UP000000547}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=34H / ATCC BAA-681 {ECO:0000313|Proteomes:UP000000547};
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic
RT   analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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}.
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DR   EMBL; CP000083; AAZ25150.1; -; Genomic_DNA.
DR   RefSeq; WP_011041850.1; NC_003910.7.
DR   ProteinModelPortal; Q487K9; -.
DR   STRING; 167879.CPS_1007; -.
DR   DNASU; 3523295; -.
DR   EnsemblBacteria; AAZ25150; AAZ25150; CPS_1007.
DR   KEGG; cps:CPS_1007; -.
DR   eggNOG; ENOG4105DY8; Bacteria.
DR   eggNOG; COG0076; LUCA.
DR   HOGENOM; HOG000282553; -.
DR   KO; K01580; -.
DR   OMA; FHKHFFQ; -.
DR   OrthoDB; POG091H05DC; -.
DR   BioCyc; CPSY167879:G1G4N-916-MONOMER; -.
DR   Proteomes; UP000000547; 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   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.
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:UP000000547};
KW   Lyase {ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000547}.
FT   MOD_RES     338    338       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   543 AA;  60524 MW;  651B51A16DB08B72 CRC64;
     MKATKRIAEA TQESLHRIFT IAEAPDSTLG RLEQEMSQNL VGFLNNHIVA SKNALTDIEQ
     DFINARIPEQ PEFVSDHMHH LLDKLVAQSV HTSSPSFIGH MTSALPSFIL PLSKLMVGLN
     QNLVKVETSK AFTPLERQVL GMMHNLVYQH DDVFYKNWMH SAEHSLGAFC SGGTVANITA
     LWVARNKLLK ADGDFRGVAR EGLHRAMRHY GYQDLAILVS DRGHYSLKKS ADILGIGQEN
     VIAIPTDEHN KIDCQKLADK CQQLAAQNIK VLAIVGVAGT TETGNIDPLD KIAEIAQQNQ
     CHFHVDAAWG GATLLSNKYR PLLKGIEQAD SVTIDAHKQM YVPMGAGLVI FKDPASVSAI
     EHHAEYILRK GSKDLGSHTL EGSRPGMAML VYSSLHIISR PGYEMLINQA IEKAEYFADI
     IHQHDDFELI TRPELCLLTY RYAPKSVQAL LARNDDEANK SVNMLLGKLT KFIQKRQRED
     GRSFVSRTRI EVSRYGGEKV IVFRVVLANP LTTKEILQGI LQEQCQLAQE SEQFLPELLQ
     AAK
//
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