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Database: UniProt
Entry: A0A140L0U1_9CLOT
LinkDB: A0A140L0U1_9CLOT
Original site: A0A140L0U1_9CLOT 
ID   A0A140L0U1_9CLOT        Unreviewed;       482 AA.
AC   A0A140L0U1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Arginine decarboxylase {ECO:0000313|EMBL:KXG74166.1};
DE            EC=4.1.1.19 {ECO:0000313|EMBL:KXG74166.1};
GN   Name=speA_2 {ECO:0000313|EMBL:KXG74166.1};
GN   ORFNames=AN619_25850 {ECO:0000313|EMBL:KXG74166.1};
OS   Thermotalea metallivorans.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Thermotalea.
OX   NCBI_TaxID=520762 {ECO:0000313|EMBL:KXG74166.1, ECO:0000313|Proteomes:UP000070456};
RN   [1] {ECO:0000313|EMBL:KXG74166.1, ECO:0000313|Proteomes:UP000070456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B2-1 {ECO:0000313|EMBL:KXG74166.1,
RC   ECO:0000313|Proteomes:UP000070456};
RA   Patel B.K.;
RT   "Draft genome sequence of the thermoanaerobe Thermotalea metallivorans, an
RT   isolate from the runoff channel of the Great Artesian Basin, Australia.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:KXG74166.1}.
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DR   EMBL; LOEE01000062; KXG74166.1; -; Genomic_DNA.
DR   RefSeq; WP_068557569.1; NZ_LOEE01000062.1.
DR   AlphaFoldDB; A0A140L0U1; -.
DR   STRING; 520762.AN619_25850; -.
DR   PATRIC; fig|520762.4.peg.2855; -.
DR   OrthoDB; 9815233at2; -.
DR   Proteomes; UP000070456; Unassembled WGS sequence.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
DR   CDD; cd00615; Orn_deC_like; 1.
DR   Gene3D; 3.90.105.10; Molybdopterin biosynthesis moea protein, domain 2; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000310; Orn/Lys/Arg_deCO2ase_major_dom.
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   PANTHER; PTHR43277; ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43277:SF3; LYSINE DECARBOXYLASE; 1.
DR   Pfam; PF01276; OKR_DC_1; 1.
DR   Pfam; PF03711; OKR_DC_1_C; 1.
DR   SUPFAM; SSF55904; Ornithine decarboxylase C-terminal domain; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:KXG74166.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070456}.
FT   DOMAIN          7..368
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|Pfam:PF01276"
FT   DOMAIN          413..469
FT                   /note="Orn/Lys/Arg decarboxylase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03711"
SQ   SEQUENCE   482 AA;  53800 MW;  27C1CEFF5D90D604 CRC64;
     MDQPIILDRL LKHGKKDMVS FHVPGHKNGK IYERYNYKNF TGQWLSLDVT EIPGMDNLHA
     PEDMIKEAQE RAAKFYRADH TFFLVDGTSC GIIAMLMAVA NPGDKIIVPR DCHKSVLHGL
     ILGNLIPAYI QPEVCSDTGI PMGILPETVE RAFKEHPEAK ALVITYPNYY GICSDVQEIA
     KIVHKYDKIL LVDEAHGAHL NLSEALPVPA IEAGADIAVQ STHKTLPAFT QASMLHVKSR
     KVNVDRLKMM LAMHQSTSPS YLLMASLDMA RTIVEGEGKF LMDQLLGHVE HFKKQIAAIG
     KIKILDQGLV GKLGVKAVDA TKLVIDMTEL GISGTLLEEL LRTKYHIQVE MANMSAIVAV
     STIGNDRRDF ERFIHALMGI KDGKGIAHRH IEVPLYSYRI PPMRLTPRQS IYMEKVAVDF
     TNSSGKISGE YLIPYPPGIP LLCPGEEITE EVIQYVQLLK RNGVQIIGIE DKELQKIKII
     EF
//
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