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Database: UniProt
Entry: A0A259U792_9FIRM
LinkDB: A0A259U792_9FIRM
Original site: A0A259U792_9FIRM 
ID   A0A259U792_9FIRM        Unreviewed;       489 AA.
AC   A0A259U792;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Arginine decarboxylase {ECO:0000313|EMBL:OZC13996.1};
DE            EC=4.1.1.19 {ECO:0000313|EMBL:OZC13996.1};
GN   Name=speA {ECO:0000313|EMBL:OZC13996.1};
GN   ORFNames=SPACI_54280 {ECO:0000313|EMBL:OZC13996.1};
OS   Sporomusa acidovorans DSM 3132.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Sporomusa.
OX   NCBI_TaxID=1123286 {ECO:0000313|EMBL:OZC13996.1, ECO:0000313|Proteomes:UP000216052};
RN   [1] {ECO:0000313|EMBL:OZC13996.1, ECO:0000313|Proteomes:UP000216052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3132 {ECO:0000313|EMBL:OZC13996.1,
RC   ECO:0000313|Proteomes:UP000216052};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Sporomusa acidovorans DSM 3132.";
RL   Submitted (FEB-2016) 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:OZC13996.1}.
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DR   EMBL; LSLL01000145; OZC13996.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A259U792; -.
DR   STRING; 112900.SAMN04488499_103830; -.
DR   Proteomes; UP000216052; Unassembled WGS sequence.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
DR   CDD; cd00615; Orn_deC_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 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   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43277; ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43277:SF4; ARGININE 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:OZC13996.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216052}.
FT   DOMAIN          8..371
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|Pfam:PF01276"
FT   DOMAIN          403..476
FT                   /note="Orn/Lys/Arg decarboxylase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03711"
SQ   SEQUENCE   489 AA;  52954 MW;  27864BDD620B67EE CRC64;
     MLDQTKVPLL EAMNSYASDG VIPFHTPGHK MGKGIHPLFQ EAVTAKALKL DLADMAELDD
     LHEPHGPIKE AQDLAADLYG ADYSYFMVNG TTGGIYSMIL TLAGPGDKLI IPRNSHRSII
     GGIILSGAIP VFMQPEVDND LGLAMGVTPE TVAESLKQHP DAKGVLLINP TYYGVATDLK
     KIVDIAHSQD IPVIVDEAHG PHLKFSPRLP MQALDAGADI VAQSTHKIIG AMTQCSLVHC
     RKDRIRVPRL KAMLQLVQST SPNYILMASL DVARMQMATA GRTLIERAVD LANQARREIN
     KIPGLYCFGN EKAGNPGVFR IDPTKVTVTV KGLGITGAEA EQILRHQYKI QVELADIYNI
     LFLITIGDSE QEVQALVAAL KDLAATHQGS HDVSALPEIC QAGRYPALPK QIISPRDALF
     GNTCRVPFAD AAGKICAEIV TFYPPGIPIL CPGERITQEI INYCHVLQNA GLHISGPEDY
     LLKTIKVVD
//
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