ID A0A6S6LX23_9BACT Unreviewed; 635 AA. AC A0A6S6LX23; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 28-JUN-2023, entry version 11. 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 ORFNames=GEOBRER4_n1332 {ECO:0000313|EMBL:BCG46532.1}; OS Citrifermentans bremense. OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales; OC Geobacteraceae; Citrifermentans. OX NCBI_TaxID=60035 {ECO:0000313|EMBL:BCG46532.1, ECO:0000313|Proteomes:UP000515472}; RN [1] {ECO:0000313|EMBL:BCG46532.1, ECO:0000313|Proteomes:UP000515472} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R4 {ECO:0000313|EMBL:BCG46532.1, RC ECO:0000313|Proteomes:UP000515472}; RA Meng L., Yoshida N.; RT "Interaction of electrochemicaly active bacteria, Geobacter bremensis R4 on RT different carbon anode."; RL Submitted (JUN-2020) 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; Evidence={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, ECO:0000256|PIRSR:PIRSR001336-50}; 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 --------------------------------------------------------------------------- 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; AP023213; BCG46532.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6S6LX23; -. DR KEGG; gbn:GEOBRER4_12820; -. DR UniPathway; UPA00186; UER00284. DR Proteomes; UP000515472; Chromosome. DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-UniRule. 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-UniRule. 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 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; 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 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}; KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01417, KW ECO:0000256|PIRSR:PIRSR001336-50}; KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066, ECO:0000256|HAMAP- KW Rule:MF_01417}. FT DOMAIN 86..342 FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal" FT /evidence="ECO:0000259|Pfam:PF02784" FT DOMAIN 372..449 FT /note="Arginine decarboxylase helical bundle" FT /evidence="ECO:0000259|Pfam:PF17810" FT DOMAIN 584..633 FT /note="Arginine decarboxylase C-terminal helical" FT /evidence="ECO:0000259|Pfam:PF17944" FT ACT_SITE 502 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50" FT BINDING 282..292 FT /ligand="substrate" 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, FT ECO:0000256|PIRSR:PIRSR001336-50" SQ SEQUENCE 635 AA; 71685 MW; A58AC59F83EFC1EA CRC64; MAKWTINDSS KIYNIDNWGA ELFSINKKGN VCVHPSPNSK YSIDLKVLVD DLIKRKIKPP ILLRFMNILE GRIASISRVF KNAISDNNYP AKYQTFYPIK VNQQRQVVEA IANFGKKYNI GLEVGSKPEL VAAISMSTGN NLPILCNGYK DTEFIETVLF ATRVGYDITI VVEKLFELEK IVEVSKRTGI VPKLGIRVKL SSKGIGKWST SGGDDAKFGL RISELIAAIE MLKQNDMLDC VKLLHFHVGS QITKIDKIKN ALIEGTRIYA EMRKLGVNLE FLDIGGGLGV DYDGSKSSYF SSVNYSLEEY ANDVIYQVKN ICDDAGVPCP NIISESGRAT VAHYSVLVTD VLNNNPQTLM PDFESILTEP EKLSPTVKKL VDIYKSIDKH SLREDYHDTI QLIQESVSLF NLGYLNMAER ANAEWICTKI IRKINSIVEK MKPIPDELQN FQLSLRQTYF ANFSLFQSIP DSWAIDQLFP IVPIQRLDEK PDVSASIADI TCDSDGEITS FVGENGRTKA LPLHKIKVDE QYYIGFFLIG AYQEILGDMH NLFGDTNAVH ITFNKKTNYK IDTVITGDAT WESLKYVQYD SQEILKRVRN NLEKDVSLQK VSIEESSHFL ELLDKTLQSY TYLGE //