ID SPEA_SHEHH Reviewed; 637 AA.
AC B0TQX3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 86.
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=Shal_1803;
OS Shewanella halifaxensis (strain HAW-EB4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=458817;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB4;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC agmatine from L-arginine: step 1/1. {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; CP000931; ABZ76368.1; -; Genomic_DNA.
DR RefSeq; WP_012276901.1; NC_010334.1.
DR AlphaFoldDB; B0TQX3; -.
DR SMR; B0TQX3; -.
DR STRING; 458817.Shal_1803; -.
DR KEGG; shl:Shal_1803; -.
DR eggNOG; COG1166; Bacteria.
DR HOGENOM; CLU_027243_1_0_6; -.
DR OrthoDB; 9802658at2; -.
DR UniPathway; UPA00186; UER00284.
DR Proteomes; UP000001317; 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; 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 3: Inferred from homology;
KW Decarboxylase; Lyase; Magnesium; Metal-binding; Polyamine biosynthesis;
KW Pyridoxal phosphate; Spermidine biosynthesis.
FT CHAIN 1..637
FT /note="Biosynthetic arginine decarboxylase"
FT /id="PRO_1000087407"
FT BINDING 286..296
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
FT MOD_RES 101
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
SQ SEQUENCE 637 AA; 71120 MW; 17A13A3F53418DA9 CRC64;
MSNWSIDDAR ASYNVNHWSQ GLYGISDDGE VTVSPDPSRP ECKIGLNEMA KDMVKSGVAL
PVLVRFPQIL HHRVNSLCQA FNQAIQKYQY ENDYLLVYPI KVNQQQTVVE EILASQVEKE
VPQLGLEAGS KPELMAVLAM AQKASSVIIC NGYKDKEYIR LALIGEKLGH KVYIVLEKIS
ELKVVLEQAK ELGVTPRLGL RVRLAFQGKG KWQASGGEKS KFGLSAAQVL QVITSLKQEN
MLDSLELLHF HLGSQIANIR DIRQGVSEAG RFYCELMKLG ANVKCFDVGG GLAVDYDGTR
SQSSHSMNYG LTEYANNIVS VLTDMCKEYE QPMPRIISES GRYLTAHHAV LLTDVIGTEA
YKPEDIQPPA EDAPQLLHNM WQSWVEVSGK ADQRALIEIF HDCQSDLTEV HSLFAVGQVG
LAERAWAEQV NLRVCYELQG SMSAKYRFHR PIIDELNEKL ADKFFVNFSL FQSLPDAWGI
DQVFPVMPLS GLDKAPESRA VMLDITCDSD GTIDQYVDGQ GIETTLPVPA WTQESPYLIG
FFLVGAYQEI LGDMHNLFGD TNSAVVRLDE DARTNVESVL AGDTVADVLR YVNLDAVSFM
RTYEELVNKH IAEDERANIL EELQLGLKGY TYLEDFS
//
