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Database: UniProt
Entry: A0A0W0W137_9GAMM
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ID   A0A0W0W137_9GAMM        Unreviewed;       628 AA.
AC   A0A0W0W137;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=arginine decarboxylase {ECO:0000256|ARBA:ARBA00012426};
DE            EC=4.1.1.19 {ECO:0000256|ARBA:ARBA00012426};
GN   Name=speA {ECO:0000313|EMBL:KTD26144.1};
GN   ORFNames=Llan_0039 {ECO:0000313|EMBL:KTD26144.1};
OS   Legionella lansingensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=45067 {ECO:0000313|EMBL:KTD26144.1, ECO:0000313|Proteomes:UP000054869};
RN   [1] {ECO:0000313|EMBL:KTD26144.1, ECO:0000313|Proteomes:UP000054869}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49751 {ECO:0000313|EMBL:KTD26144.1,
RC   ECO:0000313|Proteomes:UP000054869};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the biosynthesis of agmatine from arginine.
CC       {ECO:0000256|ARBA:ARBA00002257}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR001336-50};
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       SpeA subfamily. {ECO:0000256|ARBA:ARBA00008357}.
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:KTD26144.1}.
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DR   EMBL; LNYI01000001; KTD26144.1; -; Genomic_DNA.
DR   RefSeq; WP_028373410.1; NZ_LT906451.1.
DR   AlphaFoldDB; A0A0W0W137; -.
DR   STRING; 45067.Llan_0039; -.
DR   PATRIC; fig|45067.4.peg.40; -.
DR   eggNOG; COG1166; Bacteria.
DR   OrthoDB; 9802658at2; -.
DR   Proteomes; UP000054869; Unassembled WGS sequence.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
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-KW.
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   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 {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KTD26144.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR001336-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054869};
KW   Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066}.
FT   DOMAIN          88..339
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          365..447
FT                   /note="Arginine decarboxylase helical bundle"
FT                   /evidence="ECO:0000259|Pfam:PF17810"
FT   DOMAIN          575..624
FT                   /note="Arginine decarboxylase C-terminal helical"
FT                   /evidence="ECO:0000259|Pfam:PF17944"
FT   ACT_SITE        497
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         98
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001336-50"
SQ   SEQUENCE   628 AA;  70098 MW;  91A27C157F940C1C CRC64;
     MITKVVDDTN LYNIDHWGEG YFTINARGNI EVSKNTESRG VELQAIVNAA SRAGLQLPLL
     IRFTDILHDR VLKINEAFAE AIVENDYHGS YKLVYPIKVN QESSVVRELL KAPKYPVGLE
     AGSKPELMAV IGLLGQIPST IVCNGYKDSS YVRTALIAQQ MGHDVFIVIE KRSELDIILK
     ESARLDIKPK IGVRVRLVTK GAGKWENTGG VKSKFGLNAE QVLDLIKQLK NHNSLDCLQL
     MHCHLGSQIA NIHDIRHCMQ EVARYYIELR RLQAPITTID VGGGLGVDYE GTHSTTDCSM
     NYSIKEYATN ILLAIRPLCE EANMPEPNII SESGRALTAH HAVLITNITD VELVKKTWEL
     PVIAADDSHV IRDIWDTYQS MSESSASEIY NYATLALDEA HSMFKHGVLS LEEKAKVEQF
     FTAICFGIQQ QLDESNPGDS ELINQINERM AAKIFCNLSF FQSIPDAWAI GQIFPVAPIS
     HLTEKPSMHS VLQDLTCDSD GTIKEYTGSD SINTTLLLPQ FVPENPYAIA FFLVGAYQEI
     LGNLHNLFGD TNSLDVKLLE DGQFDITDLI SGDTVTNVLN YAHFDTKKLL LSYEKQLIHA
     ELSSEKIQTY LNELRSIFSQ LTYLDGNK
//
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