ID K6YR67_9ALTE Unreviewed; 639 AA.
AC K6YR67;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 55.
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:GAC19153.1};
GN ORFNames=GARC_2186 {ECO:0000313|EMBL:GAC19153.1};
OS Paraglaciecola arctica BSs20135.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=493475 {ECO:0000313|EMBL:GAC19153.1, ECO:0000313|Proteomes:UP000006327};
RN [1] {ECO:0000313|EMBL:GAC19153.1, ECO:0000313|Proteomes:UP000006327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSs20135 {ECO:0000313|EMBL:GAC19153.1,
RC ECO:0000313|Proteomes:UP000006327};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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:GAC19153.1}.
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DR EMBL; BAEO01000027; GAC19153.1; -; Genomic_DNA.
DR RefSeq; WP_007619658.1; NZ_BAEO01000027.1.
DR AlphaFoldDB; K6YR67; -.
DR STRING; 493475.GARC_2186; -.
DR eggNOG; COG1166; Bacteria.
DR OrthoDB; 9802658at2; -.
DR Proteomes; UP000006327; 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; 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, ECO:0000313|EMBL:GAC19153.1};
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:UP000006327};
KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066}.
FT DOMAIN 96..346
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 374..454
FT /note="Arginine decarboxylase helical bundle"
FT /evidence="ECO:0000259|Pfam:PF17810"
FT DOMAIN 584..637
FT /note="Arginine decarboxylase C-terminal helical"
FT /evidence="ECO:0000259|Pfam:PF17944"
FT ACT_SITE 504
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 104
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001336-50"
SQ SEQUENCE 639 AA; 72176 MW; 56061C6697EE6598 CRC64;
MPRTKKWTID DSENIYRVKR WGDGYFEIGQ NGNLHITPDP SNTDMRIDFK AVIDEIKQEG
IQFPLVVRFH DILRSQVALL NKTFQNTLKE AEYNGGYMGV YPIKVNQMRE VVEEIVDAGA
PFNYGLEAGS KAELLTVMAL NTNTESLTIL NGYKDEEFMR LALLSRKLGR KTIVVIEKFS
ELVLLVRIAE ELGVAPIVGI RSKMTVKGRG KWASSGGDRA KFGLTISEMI NAARYLEEHG
MADCLKLLHF HIGSQLTDIR AVKESIAEGA MIYSELHRMG FKLEYVDVGG GLGIDYDGSQ
STNDSSRNYS MQEYVADIVY GMKQVCDLED VPHPILVSES GRAITAHHSC VVTQVVGEIK
AHGAGIATKL VDGEHVLVSD MRELIEIIDN QNNLQEIFND ASQFKEQALH AFKLRVISLE
ELAKIETLYW QIMGKVQLRI KDAEFVPEEM QELDYALSSQ YLCNFSVFQS AADTWAIDQI
LPVVPLTRMN EKPTINCSLV DITCDSDGKL DQFISEYGIS NIVPMHDLKP DEDYYLGLFL
TGAYQDVMGD MHNLFGRLNE VHIFSHDDDP KDFYIEEMVH GSSVEDVLSI MQYHPSSMAK
SVKKMIDEHV AQGQMQPREG VKWTDFYEDC LKGYTYLKT
//
