SPEA_BACTN
ID SPEA_BACTN Reviewed; 630 AA.
AC Q8A2B1;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Biosynthetic arginine decarboxylase {ECO:0000255|HAMAP-Rule:MF_01417};
DE Short=ADC {ECO:0000255|HAMAP-Rule:MF_01417};
DE EC=4.1.1.19 {ECO:0000255|HAMAP-Rule:MF_01417};
GN Name=speA {ECO:0000255|HAMAP-Rule:MF_01417}; OrderedLocusNames=BT_3394;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
CC -!- FUNCTION: Catalyzes the biosynthesis of agmatine from arginine.
CC {ECO:0000255|HAMAP-Rule:MF_01417}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-arginine = agmatine + CO2; Xref=Rhea:RHEA:17641,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:58145; EC=4.1.1.19; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01417};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01417};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01417};
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC SpeA subfamily. {ECO:0000255|HAMAP-Rule:MF_01417}.
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DR EMBL; AE015928; AAO78500.1; -; Genomic_DNA.
DR RefSeq; NP_812306.1; NC_004663.1.
DR RefSeq; WP_008767598.1; NZ_UYXG01000003.1.
DR AlphaFoldDB; Q8A2B1; -.
DR SMR; Q8A2B1; -.
DR STRING; 226186.BT_3394; -.
DR PaxDb; Q8A2B1; -.
DR PRIDE; Q8A2B1; -.
DR DNASU; 1075986; -.
DR EnsemblBacteria; AAO78500; AAO78500; BT_3394.
DR GeneID; 60924573; -.
DR KEGG; bth:BT_3394; -.
DR PATRIC; fig|226186.12.peg.3462; -.
DR eggNOG; COG1166; Bacteria.
DR HOGENOM; CLU_027243_1_0_10; -.
DR InParanoid; Q8A2B1; -.
DR OMA; AVEYTQH; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0008792; F:arginine decarboxylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR GO; GO:0033388; P:putrescine biosynthetic process from arginine; IBA:GO_Central.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06830; PLPDE_III_ADC; 1.
DR Gene3D; 2.40.37.10; -; 1.
DR Gene3D; 3.20.20.10; -; 1.
DR HAMAP; MF_01417; SpeA; 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; IPR022657; De-COase2_CS.
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; PTHR43295; 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; SSF50621; 1.
DR SUPFAM; SSF51419; SSF51419; 1.
DR TIGRFAMs; TIGR01273; speA; 1.
DR PROSITE; PS00878; ODR_DC_2_1; 1.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Magnesium; Metal-binding; Polyamine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Spermidine biosynthesis.
FT CHAIN 1..630
FT /note="Biosynthetic arginine decarboxylase"
FT /id="PRO_0000149957"
FT BINDING 281..291
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
FT MOD_RES 99
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
SQ SEQUENCE 630 AA; 71246 MW; C124255A68131F19 CRC64;
MRKWRIEDSE ELYNITGWGT SYFSINDAGH VVVTPRRDGV TVDLKELVDE LQLRDVASPM
LLRFPDILDN RIEKMSSCFK QAAEEYGYKA ENFIIYPIKV NQMRPVVEEI ISHGKKFNLG
LEAGSKPELH AVIAVNTDSD SLIVCNGYKD ESYIELALLA QKMGKRIFLV VEKMNELKLI
AKMAKQLNVQ PNIGIRIKLA SSGSGKWEES GGDASKFGLT SSELLEALDF MESKGLKDCL
KLIHFHIGSQ VTKIRRIKTA LREASQFYVQ LHSMGFNVEF VDIGGGLGVD YDGTRSSNSE
GSVNYSIQEY VNDSISTLVD VSDKNGIPHP NIITESGRAL TAHHSVLIFE VLETATLPEW
DDEEEIAPDA HELVQELYSI WDSLNQNKML EAWHDAQQIR EEALDLFSHG IVDLKTRAQI
ERLYWSITRE INQIAGGLKH APDEFRGLSK LLADKYFCNF SLFQSLPDSW AIDQIFPIMP
IQRLDEKPER SATLQDITCD SDGKIANFIS TRNVAHYLPV HSLKKTEPYY LAVFLVGAYQ
EILGDMHNLF GDTNAVHVSV NEKGYNIEQI IDGETVAEVL DYVQYNPKKL VRTLETWVTK
SVKEGKISLE EGKEFLSNYR SGLYGYTYLE