ID Q1N474_9GAMM Unreviewed; 647 AA.
AC Q1N474;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 90.
DE RecName: Full=arginine decarboxylase {ECO:0000256|ARBA:ARBA00012426};
DE EC=4.1.1.19 {ECO:0000256|ARBA:ARBA00012426};
GN ORFNames=RED65_14882 {ECO:0000313|EMBL:EAT12991.1};
OS Bermanella marisrubri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Bermanella.
OX NCBI_TaxID=207949 {ECO:0000313|EMBL:EAT12991.1, ECO:0000313|Proteomes:UP000004263};
RN [1] {ECO:0000313|EMBL:EAT12991.1, ECO:0000313|Proteomes:UP000004263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RED65 {ECO:0000313|EMBL:EAT12991.1,
RC ECO:0000313|Proteomes:UP000004263};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA Venter J.C.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the biosynthesis of agmatine from arginine.
CC {ECO:0000256|ARBA:ARBA00002257}.
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:PIRSR001336-50};
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:EAT12991.1}.
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DR EMBL; AAQH01000003; EAT12991.1; -; Genomic_DNA.
DR RefSeq; WP_007018062.1; NZ_CP051183.1.
DR AlphaFoldDB; Q1N474; -.
DR STRING; 207949.RED65_14882; -.
DR HOGENOM; CLU_027243_1_0_6; -.
DR OrthoDB; 9802658at2; -.
DR Proteomes; UP000004263; Unassembled WGS sequence.
DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06830; PLPDE_III_ADC; 1.
DR Gene3D; 1.10.287.3440; -; 1.
DR Gene3D; 1.20.58.930; -; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR040634; Arg_decarb_HB.
DR InterPro; IPR041128; Arg_decarbox_C.
DR InterPro; IPR002985; Arg_decrbxlase.
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 NCBIfam; TIGR01273; speA; 1.
DR PANTHER; PTHR43295; ARGININE DECARBOXYLASE; 1.
DR PANTHER; PTHR43295:SF9; BIOSYNTHETIC ARGININE DECARBOXYLASE; 1.
DR Pfam; PF17810; Arg_decarb_HB; 1.
DR Pfam; PF17944; Arg_decarbox_C; 1.
DR Pfam; PF02784; Orn_Arg_deC_N; 1.
DR PIRSF; PIRSF001336; Arg_decrbxlase; 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, ECO:0000313|EMBL:EAT12991.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR001336-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000004263};
KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066}.
FT DOMAIN 90..354
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 380..460
FT /note="Arginine decarboxylase helical bundle"
FT /evidence="ECO:0000259|Pfam:PF17810"
FT DOMAIN 589..642
FT /note="Arginine decarboxylase C-terminal helical"
FT /evidence="ECO:0000259|Pfam:PF17944"
FT ACT_SITE 511
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 112
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001336-50"
SQ SEQUENCE 647 AA; 72749 MW; FC7CAEB2E76FB469 CRC64;
MRTKPLAAPP HEAPWSAQDS ADLYGVNDWG CDFFKVSDNG ELEVQVDFKD HTVSVPLIQI
IEGMQERGLE MPAILRIENL LDARISALNE AFARAIQSYQ YGNVYRGVFP IKVNQQCHVV
EEIADFGSRY HHGLEAGSKA ELIIALSKLH DNESMIVCNG YKDAEFIELG LYAKEMGINC
IFVLESLKEL PIILERSEAL GIEPLLGVRI RSSVTVDGHW NEDSGDRSIF GMSTHSLVRV
VEELKQANML HCLQLLHCHL GSQIPNIRNI RMGVMEACRF YSGLIEQGAP MGYLDLGGGL
AVDYEGASSN HTHSMNYQLD EYCNNIVETI QECLDPENIP HPVIVTESGR ATVAYSSMLL
FNTLDVRTYE PAPLPESLAD DASSTLQSLW QVNQDVGAEN YQECYNDALF YRDEIQSLFR
RGQASLSERA IAENIALSIF QKVAKEIRSS ERVPEEMQHL PQMLADIYYG NFSVFQSLPD
TWAIDQVFPV MPIHRLDEKP TRDAMLADLT CDCDGKIDVF ATAEGTSSTL ALHSLKEEEE
YYLGVFLVGA YQETLGDLHN LFGDTHVVSV AIREDGRFDF VREIHGDSIA DVLSYVEYDP
RIMSEELRQR AEKAVRQGRI TPARRKQMLK AFKASLDGYT YFERGTL
//
