ID A0A1F5NU51_9BACT Unreviewed; 470 AA.
AC A0A1F5NU51;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 03-MAY-2023, entry version 21.
DE RecName: Full=arginine decarboxylase {ECO:0000256|ARBA:ARBA00012426};
DE EC=4.1.1.19 {ECO:0000256|ARBA:ARBA00012426};
GN ORFNames=A2720_01345 {ECO:0000313|EMBL:OGE81168.1};
OS Candidatus Doudnabacteria bacterium RIFCSPHIGHO2_01_FULL_46_24.
OC Bacteria; Candidatus Doudnabacteria.
OX NCBI_TaxID=1817825 {ECO:0000313|EMBL:OGE81168.1, ECO:0000313|Proteomes:UP000178892};
RN [1] {ECO:0000313|EMBL:OGE81168.1, ECO:0000313|Proteomes:UP000178892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
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:OGE81168.1}.
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DR EMBL; MFEL01000010; OGE81168.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5NU51; -.
DR STRING; 1817825.A2720_01345; -.
DR Proteomes; UP000178892; Unassembled WGS sequence.
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; IPR022643; De-COase2_C.
DR InterPro; IPR022644; De-COase2_N.
DR InterPro; IPR022653; De-COase2_pyr-phos_BS.
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 Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR PRINTS; PR01180; ARGDCRBXLASE.
DR PRINTS; PR01179; ODADCRBXLASE.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS00878; ODR_DC_2_1; 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 Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066}.
FT DOMAIN 82..327
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 328..426
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 394
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 107
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 470 AA; 54231 MW; F238B246B187C4A1 CRC64;
MLYHKRVKKN QTVRKRKKKN GFKKFWRLGL EEFNTQNFDI GPDGELIVRE GNYQYNVHDL
VKKYGSPTEI VFPTIMENRV RDLIETFNAY IKILGYKGRF YYHYAMKANQ TKEFVLPAVA
EGANLDVASA NELYLVKRMI EQDKFNRKIR VICNGPKTEK YISLIEELKG KGLIVVPIIE
DYNELERLKK FKGEVGIRVN LDIKVQAHWD KKFNRYGFTE EELLKIGKVR NLSTLHYHIS
KQIITIKGFT KPLKRALRLF AGMKEKNPGL MILDIGGGAG IPFEKKKHFY SGKSLIHQIV
KTAKKECDKL GIRHPNLIVE WGSYVAAPAQ ITIYKIITEK DVSVKNHKKW YVVDGSFMND
LLDTWAIHQK WHVVPVNCMN SRKLQPVWFA GSSCDSDDKY TAGGDYIPMP RLEDCDELFV
AFFDTGAYQD ALASHHCLLS SPAKLIAQNG EIKVARRRET AEDVGRQFGW
//
