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Database: UniProt
Entry: Q5QTW2_IDILO
LinkDB: Q5QTW2_IDILO
Original site: Q5QTW2_IDILO 
ID   Q5QTW2_IDILO            Unreviewed;       636 AA.
AC   Q5QTW2;
DT   04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT   04-JAN-2005, sequence version 1.
DT   24-JAN-2024, entry version 117.
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:AAV82053.1};
GN   OrderedLocusNames=IL1213 {ECO:0000313|EMBL:AAV82053.1};
OS   Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=283942 {ECO:0000313|EMBL:AAV82053.1, ECO:0000313|Proteomes:UP000001171};
RN   [1] {ECO:0000313|EMBL:AAV82053.1, ECO:0000313|Proteomes:UP000001171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR
RC   {ECO:0000313|Proteomes:UP000001171};
RX   PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA   Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA   Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA   Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA   Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT   "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT   loihiensis reveals amino acid fermentation as a source of carbon and
RT   energy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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}.
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DR   EMBL; AE017340; AAV82053.1; -; Genomic_DNA.
DR   RefSeq; WP_011234464.1; NC_006512.1.
DR   AlphaFoldDB; Q5QTW2; -.
DR   STRING; 283942.IL1213; -.
DR   KEGG; ilo:IL1213; -.
DR   eggNOG; COG1166; Bacteria.
DR   HOGENOM; CLU_027243_1_0_6; -.
DR   OMA; AVEYTQH; -.
DR   OrthoDB; 9802658at2; -.
DR   Proteomes; UP000001171; Chromosome.
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; 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   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; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 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};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
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:UP000001171};
KW   Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066}.
FT   DOMAIN          93..343
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          369..450
FT                   /note="Arginine decarboxylase helical bundle"
FT                   /evidence="ECO:0000259|Pfam:PF17810"
FT   DOMAIN          581..633
FT                   /note="Arginine decarboxylase C-terminal helical"
FT                   /evidence="ECO:0000259|Pfam:PF17944"
FT   ACT_SITE        500
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         101
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001336-50"
SQ   SEQUENCE   636 AA;  71910 MW;  5C855303A0A4CE9E CRC64;
     MSDWNIDQAE ELYGVNRWGA GYFSIGENGN IQIRPNHRLP DVTIDMKEVV DEIISEGIQF
     PAVIRFHDIL RSQVEIINET FGKQIEEANY QGQYCGVFPI KVNQMREVVE EIMDAGEPYN
     YGLEAGSKPE LMAVMAYNDN PEALTILNGY KDKDYLTLAL LGRQLKRKMI IVIEKFSELE
     MLIPLAKQMG VKPMIGLRSK MMVKSSGKWA GSSGDRAKFG LSIAEILNVI ERLREEDMLH
     CAKLLHFHIG SQLSDIRKIK EAVNEGARLY AKLVLEGMPL EYLDIGGGLG IDYDGTSTTN
     DSSRNYSTEE YVADVVWGVK QICDLEKVPH PNLVSESGRA MTAHHSCVVT NIVGEMKPAG
     TQYDISASSD EHILVKNMRE LHSSGDQFHP QERYNDAAGY KQNAYEAFKL GILSLNEMAK
     LDTMYWQILA DIHHSLDKDT YVMQELEELE DMLASQYLCN FSVFQSAADT WAIGQVLPVV
     PISRLNEQPE VRCSIVDITC DSDGKLSKYI EGTDISDHIP MHNLRKGEDY HVGLFLTGAY
     QDVMGDMHNL FGRLTEVHVY CHDDEPGDFY IEEVVPGTSA EKVLQTMQYN TEYMAKTVKK
     QIDRQVRKGS LAPREGVRWT NFYEHCLAGS TYLRVE
//
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