UniProt: A0A126V5J4

Database: UniProt
Entry: A0A126V5J4_9RHOB

LinkDB:  A0A126V5J4_9RHOB 
Original site:  A0A126V5J4_9RHOB

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (14)   
   InterPro (9)   
   Pfam (3)   
   PROSITE (2)   
All databases (21)   

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ID   A0A126V5J4_9RHOB        Unreviewed;       629 AA.
AC   A0A126V5J4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=arginine decarboxylase {ECO:0000256|ARBA:ARBA00012426};
DE            EC=4.1.1.19 {ECO:0000256|ARBA:ARBA00012426};
GN   ORFNames=RC74_05695 {ECO:0000313|EMBL:AML53543.1};
OS   Falsihalocynthiibacter arcticus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Falsihalocynthiibacter.
OX   NCBI_TaxID=1579316 {ECO:0000313|EMBL:AML53543.1, ECO:0000313|Proteomes:UP000070371};
RN   [1] {ECO:0000313|EMBL:AML53543.1, ECO:0000313|Proteomes:UP000070371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 20958 {ECO:0000313|EMBL:AML53543.1};
RA   Lee Y.M., Baek K., Lee H.K., Shin S.C.;
RT   "Complete genome sequence of Halocynthiibacter arcticus PAMC 20958t from
RT   arctic marine sediment.";
RL   Submitted (FEB-2016) 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}.
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DR   EMBL; CP014327; AML53543.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A126V5J4; -.
DR   STRING; 1579316.RC74_05695; -.
DR   KEGG; hat:RC74_05695; -.
DR   OrthoDB; 9802658at2; -.
DR   Proteomes; UP000070371; 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; 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:UP000070371};
KW   Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066}.
FT   DOMAIN          88..342
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          367..437
FT                   /note="Arginine decarboxylase helical bundle"
FT                   /evidence="ECO:0000259|Pfam:PF17810"
FT   DOMAIN          575..628
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         100
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001336-50"
SQ   SEQUENCE   629 AA;  69830 MW;  E3A2B09BCB6A7B05 CRC64;
     MTHDNTAANS VYAIERWGKD LVGVLPNGDL GLRNPLKPDA PMVSLPVILQ DLEERGVHAP
     LLLRVSSFLE SSIRALNESF ASAIKRAGYK NEYRAVFPVK VNQQAQVISR IVEFGKPYSH
     GLEAGSKPEL VIALAQPLAH DALIVCNGVK DAEFIRLAIL SRKLGFNTVI VLESPKELQT
     VLAVVKELGE EPQLGVRVKL SNRISGNWAE SSGDRSTFGM HTDQLVDVID SLKEAGLIHC
     LKFQHSHLGS QIPDVNDVRR ATGEACRYFV ELTREGAPLT HLDLGGGLGV DYTGEKSTNE
     NSINYSVDEY CTNIVETVSY ALDEAKIPHP ILVTESGRAV VATSSMLIFN VLEATLYDSH
     NPTVPAAEDH HFVSDLAAVS GYLEPQRLQE CINDSSFYRN ELRALFRRGY IDLRQMARAE
     RIYLHLMSKI KSLAPEVGTA PDVDAHLEQL ADIYHCNFSL FQSLPDVWAI DQVHPLVPLQ
     MLNVAPDRRA VLSDITCDSD GKIDKFILAD GISPSLPVHT LDESKPYYIG VFYVGAYQET
     LGDLHNLFGD TNVATIDLRD DGSFDLLHEQ EGDTIAEVLS YVEYDPRDCV DAFRARIDNE
     ISHKRLNPKD RKTLLAAYRD SINGYTYYE
//

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