SPEA_VIBVY
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 03-AUG-2022, entry version 104.
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; Proteobacteria; 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;
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; 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 EnsemblBacteria; BAC94750; BAC94750; BAC94750.
DR KEGG; vvy:VV1986; -.
DR eggNOG; COG1166; Bacteria.
DR HOGENOM; CLU_027243_1_0_6; -.
DR OMA; AVEYTQH; -.
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; 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; IPR022644; De-COase2_N.
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; SSF51419; SSF51419; 1.
DR TIGRFAMs; TIGR01273; speA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Lyase; Magnesium; Metal-binding;
KW Polyamine biosynthesis; Pyridoxal phosphate; Reference proteome;
KW 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
