ID SPEA_VIBVY Reviewed; 640 AA. AC Q7MK24; DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 27-MAR-2024, entry version 111. 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=VV1986; OS Vibrio vulnificus (strain YJ016). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=196600; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YJ016; RX PubMed=14656965; DOI=10.1101/gr.1295503; RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L., RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P., RA Lee C.-T., Hor L.-I., Tsai S.-F.; RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen."; RL Genome Res. 13:2577-2587(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; Evidence={ECO:0000255|HAMAP- CC 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}. 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; BA000037; BAC94750.1; -; Genomic_DNA. DR PDB; 3N2O; X-ray; 2.30 A; A/B/C/D=1-640. DR PDBsum; 3N2O; -. DR AlphaFoldDB; Q7MK24; -. DR SMR; Q7MK24; -. DR STRING; 672.VV93_v1c17470; -. DR KEGG; vvy:VV1986; -. DR eggNOG; COG1166; Bacteria. DR HOGENOM; CLU_027243_1_0_6; -. DR BRENDA; 4.1.1.19; 7786. DR EvolutionaryTrace; Q7MK24; -. DR Proteomes; UP000002675; Chromosome I. 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; IPR022644; De-COase2_N. 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; SSF51419; PLP-binding barrel; 1. PE 1: Evidence at protein level; KW 3D-structure; Decarboxylase; Lyase; Magnesium; Metal-binding; KW Polyamine biosynthesis; Pyridoxal phosphate; Spermidine biosynthesis. FT CHAIN 1..640 FT /note="Biosynthetic arginine decarboxylase" FT /id="PRO_0000149986" FT BINDING 290..300 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417" FT MOD_RES 105 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417" FT HELIX 11..18 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 21..24 FT /evidence="ECO:0007829|PDB:3N2O" FT STRAND 27..30 FT /evidence="ECO:0007829|PDB:3N2O" FT STRAND 36..38 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 50..59 FT /evidence="ECO:0007829|PDB:3N2O" FT STRAND 64..69 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 71..92 FT /evidence="ECO:0007829|PDB:3N2O" FT STRAND 98..100 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 104..106 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 110..122 FT /evidence="ECO:0007829|PDB:3N2O" FT STRAND 129..132 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 135..144 FT /evidence="ECO:0007829|PDB:3N2O" FT STRAND 146..148 FT /evidence="ECO:0007829|PDB:3N2O" FT STRAND 151..154 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 160..171 FT /evidence="ECO:0007829|PDB:3N2O" FT STRAND 175..180 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 185..196 FT /evidence="ECO:0007829|PDB:3N2O" FT STRAND 201..206 FT /evidence="ECO:0007829|PDB:3N2O" FT TURN 213..216 FT /evidence="ECO:0007829|PDB:3N2O" FT STRAND 218..221 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 230..242 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 246..248 FT /evidence="ECO:0007829|PDB:3N2O" FT STRAND 249..253 FT /evidence="ECO:0007829|PDB:3N2O" FT STRAND 258..260 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 263..282 FT /evidence="ECO:0007829|PDB:3N2O" FT STRAND 289..291 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 315..333 FT /evidence="ECO:0007829|PDB:3N2O" FT STRAND 339..342 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 345..349 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 350..352 FT /evidence="ECO:0007829|PDB:3N2O" FT STRAND 353..363 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 379..389 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 397..419 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 425..445 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 453..463 FT /evidence="ECO:0007829|PDB:3N2O" FT STRAND 466..472 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 474..477 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 479..484 FT /evidence="ECO:0007829|PDB:3N2O" FT STRAND 490..494 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 496..498 FT /evidence="ECO:0007829|PDB:3N2O" FT STRAND 501..511 FT /evidence="ECO:0007829|PDB:3N2O" FT STRAND 520..522 FT /evidence="ECO:0007829|PDB:3N2O" FT STRAND 525..532 FT /evidence="ECO:0007829|PDB:3N2O" FT STRAND 542..547 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 552..555 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 559..561 FT /evidence="ECO:0007829|PDB:3N2O" FT STRAND 566..572 FT /evidence="ECO:0007829|PDB:3N2O" FT STRAND 578..584 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 589..595 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 600..614 FT /evidence="ECO:0007829|PDB:3N2O" FT HELIX 617..632 FT /evidence="ECO:0007829|PDB:3N2O" FT STRAND 633..636 FT /evidence="ECO:0007829|PDB:3N2O" SQ SEQUENCE 640 AA; 72493 MW; 3157EA5825FFF912 CRC64; MRLDVEQTSK LDRVRADYNV HYWSQGFYGI DDQGEMYVSP RSDNAHQIQL SKIVKQLEER QLNVPVLVRF PQILHQRVHS ICDAFNQAIE EYQYPNKYLL VYPIKVNQQR EVVDEILASQ AQLETKQLGL EAGSKPELLA VLAMAQHASS VIVCNGYKDR EYIRLALIGE KLGHKVFIVL EKMSELDLVL REAKSLGVTP RLGIRIRLAS QGAGKWQASG GEKSKFGLSA SQVLNVISRL KKENQLDTLQ LVHFHLGSQM ANIRDVRNGV NESARFYCEL RTLGANITYF DVGGGLAIDY DGTRSQSSNS MNYGLVEYAR NIVNTVGDVC KDYKQPMPVI ISESGRSLTA HHAVLISNVI GTETYKPETV TEPEEDFPLL LNNMWRSWLN LHNGTDARAL IEIYNDTQSD LAEVHSQFAT GVLTLEHRAW AEQTSLRIYY ELNRLMSTKN RFHRPILDEL SERLADKFFV NFSLFQSLPD SWGIDQVFPV LPLSGLQNAA DRRAVMLDIT CDSDGAIDAY VDGQGIESTL PVPAWNEDEP YLMGFFLVGA YQEILGDMHN LFGDTHSVVV NVGDQGEINI DFINEGDTVE DMMRYVHIDV DQIRKNYHSL VSQRVDQEEQ QQILAELEQG LSGYTYLEDF //