ID   A7NM06_ROSCS            Unreviewed;       528 AA.
AC   A7NM06;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=arginine decarboxylase {ECO:0000256|ARBA:ARBA00012426};
DE            EC=4.1.1.19 {ECO:0000256|ARBA:ARBA00012426};
GN   OrderedLocusNames=Rcas_2474 {ECO:0000313|EMBL:ABU58554.1};
OS   Roseiflexus castenholzii (strain DSM 13941 / HLO8).
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC   Roseiflexaceae; Roseiflexus.
OX   NCBI_TaxID=383372 {ECO:0000313|EMBL:ABU58554.1, ECO:0000313|Proteomes:UP000000263};
RN   [1] {ECO:0000313|EMBL:ABU58554.1, ECO:0000313|Proteomes:UP000000263}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13941 / HLO8 {ECO:0000313|Proteomes:UP000000263};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Bryant D.A., Hanada S., Tsukatani Y., Richardson P.;
RT   "Complete sequence of Roseiflexus castenholzii DSM 13941.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR600183-50};
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       SpeA subfamily. {ECO:0000256|ARBA:ARBA00008357}.
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DR   EMBL; CP000804; ABU58554.1; -; Genomic_DNA.
DR   RefSeq; WP_012120978.1; NC_009767.1.
DR   AlphaFoldDB; A7NM06; -.
DR   STRING; 383372.Rcas_2474; -.
DR   KEGG; rca:Rcas_2474; -.
DR   eggNOG; COG0019; Bacteria.
DR   HOGENOM; CLU_027243_2_0_0; -.
DR   OrthoDB; 9802658at2; -.
DR   Proteomes; UP000000263; Chromosome.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR002985; Arg_decrbxlase.
DR   InterPro; IPR022644; De-COase2_N.
DR   InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   PANTHER; PTHR43295; ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43295:SF9; BIOSYNTHETIC ARGININE DECARBOXYLASE; 1.
DR   Pfam; PF02784; Orn_Arg_deC_N; 1.
DR   PRINTS; PR01179; ODADCRBXLASE.
DR   SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000263};
KW   Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066}.
FT   DOMAIN          75..320
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   REGION          478..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..500
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        387
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         91
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   528 AA;  58971 MW;  035D8DA29B7AF4F1 CRC64;
     MNGQTYVTAF TNRYGVGPEG PINDFISRRG DRLLLADQID LNAMAARYGA PLEVVYCPQI
     TVQIERMREW AEAARARSGY AGDFIYAYAT KANFAEEVVR TAISSGAHYE TSAAADVAIA
     HYLWQQGVLP SDRFIFCNGS KDHAYIAAIV TLRHAGFARV VPVIDDLDEL ETLLAMCREP
     LLLGVRERHT PADVDVNHPG GERFGLTPDE IARVVERLHH TPHRLVMYHA MVGSQIEDPE
     RWNERLARSA EAYARLRQRA PSLWLFNFGG GMPTSAYSLD FRFDYAGFLD RLMTMLAAVC
     DTHHIPQPTL VGEFGRYTVA SHNVFIMEVG RVKCGQGAAP DWVLLNGSLM VALPDSLIVP
     GQEFIILPLD GWDQPVRPVR LAGRLTCDSD DFFPRPGAPP LLLPEPYPGQ KIAFFGVGAY
     QQMIAGRGGA HHCLTPEMRR IIIERDEDAL VVREIAPQNV GQIMGLLGYA RETLELPTPQ
     HERMPAERRA PREPIRAPRP ARRRNVLRNA PPVRYGAERR GWGVRVRG
//