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Database: UniProt
Entry: L1Q2V9_9CLOT
LinkDB: L1Q2V9_9CLOT
Original site: L1Q2V9_9CLOT 
ID   L1Q2V9_9CLOT            Unreviewed;       716 AA.
AC   L1Q2V9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Orn/Lys/Arg decarboxylase, major domain protein {ECO:0000313|EMBL:EKY22246.1};
GN   ORFNames=HMPREF0216_03290 {ECO:0000313|EMBL:EKY22246.1};
OS   Clostridium celatum DSM 1785.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=545697 {ECO:0000313|EMBL:EKY22246.1, ECO:0000313|Proteomes:UP000010420};
RN   [1] {ECO:0000313|EMBL:EKY22246.1, ECO:0000313|Proteomes:UP000010420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1785 {ECO:0000313|EMBL:EKY22246.1,
RC   ECO:0000313|Proteomes:UP000010420};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC       {ECO:0000256|ARBA:ARBA00010671}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKY22246.1}.
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DR   EMBL; AMEZ01000133; EKY22246.1; -; Genomic_DNA.
DR   RefSeq; WP_005216094.1; NZ_KB291715.1.
DR   AlphaFoldDB; L1Q2V9; -.
DR   STRING; 545697.HMPREF0216_03290; -.
DR   PATRIC; fig|545697.3.peg.3214; -.
DR   eggNOG; COG1982; Bacteria.
DR   HOGENOM; CLU_014292_3_0_9; -.
DR   OrthoDB; 9815233at2; -.
DR   Proteomes; UP000010420; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd00615; Orn_deC_like; 1.
DR   Gene3D; 3.40.50.220; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.90.100.10; Orn/Lys/Arg decarboxylase, C-terminal domain; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR011193; Orn/lys/arg_de-COase.
DR   InterPro; IPR000310; Orn/Lys/Arg_deCO2ase_major_dom.
DR   InterPro; IPR027464; Ornithine_deCO2ase_N.
DR   InterPro; IPR008286; Prn/Lys/Arg_de-COase_C.
DR   InterPro; IPR036633; Prn/Lys/Arg_de-COase_C_sf.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR45229:SF3; BIODEGRADATIVE ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR45229; CONSTITUTIVE ORNITHINE DECARBOXYLASE; 1.
DR   Pfam; PF01276; OKR_DC_1; 1.
DR   Pfam; PF03711; OKR_DC_1_C; 1.
DR   PIRSF; PIRSF009393; Orn_decarb; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF55904; Ornithine decarboxylase C-terminal domain; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00703; OKR_DC_1; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR009393-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010420}.
FT   DOMAIN          347..361
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS00703"
FT   MOD_RES         352
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009393-1"
SQ   SEQUENCE   716 AA;  81660 MW;  411B63AD10DA0F3D CRC64;
     MKSLKIACTE RTRNYFFTDR ETIQVGTTDY TDVAAAVVNE NDIEVINDIY DTRFGIAIFV
     IAETNDISCE INDKVYKIIT ISDLNEEIFS KELNKVADKY EEEMLPPFFN VLSEYSRRGN
     LQFACPGHQG GQYFIKHPAG RAMYEFFGEN IFKSDICNAD VDLGDLLIHE GPAMSAQAYA
     AKVYNADKTY FVMNGTSTSN SVVINAIVSP GDLVLFDRNN HKSIYNSALV SSAGKPVYLE
     TARNPFGFIG GIDAHCFNEE YLRNEAAKVD SEKAKEKRPF RLAVIQLGTY DGTIYNARQV
     VDKIGHLCDY ILFDSAWVGY EQFIPMMRDC SPLLLDLKPE DPGILHTQSI HKQQAGFSQT
     SQIHKKDSHL KGQKRYVDHK RFNNAYMLYA STSPFYPLFA ALDVNARMQD GEAGKKLWAD
     CIKVGIEARK DVLDRCTMLK PFIPPTVRGK LWQDYNAEEI ANDIEFFKFY PGEKWHSFEG
     YGENQYFVDP NKFMLTTPGI NVETGEYEEF GIPATILANY LRDHRVVPEK NDLNSILFLL
     TPAETTEKMQ GLVDHLVRFE SLIKEDAPLS KVLPKLYAKY EERYKGYTIK RLCQEMHDFY
     KENDAKTYQK LLFRRNSLPE YVMNPNEANV ELKRNNAKLV PLSDIVGEIA LEGALPYPPG
     VFCVVPGERW NTVAQKYFSI LEEGINRFPG FAPEIQGVYL EKENGKIRAY GYVLDK
//
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