ID   Q487K9_COLP3            Unreviewed;       543 AA.
AC   Q487K9;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 108.
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; Pseudomonadota; 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}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=34H {ECO:0000313|EMBL:AAZ25150.1};
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 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|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, 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   AlphaFoldDB; Q487K9; -.
DR   STRING; 167879.CPS_1007; -.
DR   DNASU; 3523295; -.
DR   KEGG; cps:CPS_1007; -.
DR   eggNOG; COG0076; Bacteria.
DR   HOGENOM; CLU_011856_0_4_6; -.
DR   Proteomes; UP000000547; Chromosome.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR03799; NOD_PanD_pyr; 1.
DR   PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES         338
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="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
//