ID A0A849MPT1_9BACT Unreviewed; 630 AA. AC A0A849MPT1; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 19-JAN-2022, entry version 2. DE RecName: Full=Biosynthetic arginine decarboxylase {ECO:0000256|HAMAP-Rule:MF_01417}; DE Short=ADC {ECO:0000256|HAMAP-Rule:MF_01417}; DE EC=4.1.1.19 {ECO:0000256|HAMAP-Rule:MF_01417}; GN Name=speA {ECO:0000256|HAMAP-Rule:MF_01417, GN ECO:0000313|EMBL:NOG68166.1}; GN ORFNames=HND41_08265 {ECO:0000313|EMBL:NOG68166.1}; OS Chlorobi bacterium. OC Bacteria; Chlorobi. OX NCBI_TaxID=2268192 {ECO:0000313|EMBL:NOG68166.1, ECO:0000313|Proteomes:UP000591485}; RN [1] {ECO:0000313|EMBL:NOG68166.1, ECO:0000313|Proteomes:UP000591485} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CHB4 {ECO:0000313|EMBL:NOG68166.1}; RA Ali M., Shaw D.R., Saikaly P.; RT "Comparative Genome-Resolved Analysis of Two Physiologically Distant RT ANAMMOX Cultures Hints Functional Redundancy in Both Ecosystems."; RL Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the biosynthesis of agmatine from arginine. CC {ECO:0000256|ARBA:ARBA00002257, ECO:0000256|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; CC Evidence={ECO:0000256|ARBA:ARBA00000009, ECO:0000256|HAMAP- CC Rule:MF_01417}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|HAMAP-Rule:MF_01417}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933, CC ECO:0000256|HAMAP-Rule:MF_01417}; CC -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis; CC agmatine from L-arginine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01417}. CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family. CC SpeA subfamily. {ECO:0000256|ARBA:ARBA00008357, ECO:0000256|HAMAP- CC Rule:MF_01417}. 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:NOG68166.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JABFFV010000013; NOG68166.1; -; Genomic_DNA. DR UniPathway; UPA00186; UER00284. DR Proteomes; UP000591485; Unassembled WGS sequence. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. 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 {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP- KW Rule:MF_01417}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01417}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01417}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01417}; KW Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115, ECO:0000256|HAMAP- KW Rule:MF_01417}; Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01417}; KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066, ECO:0000256|HAMAP- KW Rule:MF_01417}. FT DOMAIN 92..342 FT /note="Orn_Arg_deC_N" FT /evidence="ECO:0000259|Pfam:PF02784" FT DOMAIN 368..448 FT /note="Arg_decarb_HB" FT /evidence="ECO:0000259|Pfam:PF17810" FT DOMAIN 575..628 FT /note="Arg_decarbox_C" FT /evidence="ECO:0000259|Pfam:PF17944" FT REGION 282..292 FT /note="Substrate-binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01417" FT MOD_RES 100 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01417" SQ SEQUENCE 630 AA; 71262 MW; 429824800DE36303 CRC64; MRKWRAEDSS ELYNVHGWGV SYFGVNEAGN VTVQPRKNKG PEIDLKQVID EVVARDVSLP VLLRFPDILD DRIEKIALCF DKAGADYGYN GQYYSVYPIK VNQQRPVVEE LVRYGERVNI GLEAGSKPEL HAVLAIMGNP DALIICNGYK DEDYIELALL AQKMGKQIYV VVEKLNELRL INTISKRLGV RPNIGIRIKL AASGSGKWEE SGGDNSKFGL NPAELLEAVD YARNENLLDC LRLIHFHLGS QITNIRRIKS GLREVSEYYV ELMKQGCNIE FVDIGGGLGV DYDGSRSSYA SSINYSIQEY ANDAVATIVD AATRNSLPHP NLITESGRAL TAHHSVLVFN VLETAKVPEW GETDTADDTD HELVREMHGI LQNISPRAMF ESWHDAQQVR EEALDRFSLG LVDLAARAKV EKLYWSVARA VYDLSKELKN PPEELKPLQR LLAEKYFCNF SLFQSLPDSW AIDQLFPIMP IHRLCEKPTR MATLQDITCD SDGKVDRFIG GRDYRQTLPL HPMNSEPYYL AVFLVGAYQE ILGDLHNLFG DTNAVHIVIK NNTYHIENII DGETVADVLD YVQFDAKRLV RTMETWVNSS VQDGRISNHE GREFLNIYRS GLYGYTYLEE //