ID A0A1G4ZH68_9BURK Unreviewed; 765 AA.
AC A0A1G4ZH68;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Arginine decarboxylase {ECO:0000313|EMBL:SCX64999.1};
GN ORFNames=SAMN03159363_2483 {ECO:0000313|EMBL:SCX64999.1};
OS Variovorax sp. EL159.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1566270 {ECO:0000313|EMBL:SCX64999.1, ECO:0000313|Proteomes:UP000199507};
RN [1] {ECO:0000313|EMBL:SCX64999.1, ECO:0000313|Proteomes:UP000199507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EL159 {ECO:0000313|EMBL:SCX64999.1,
RC ECO:0000313|Proteomes:UP000199507};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC {ECO:0000256|ARBA:ARBA00010671}.
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DR EMBL; FMUJ01000003; SCX64999.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4ZH68; -.
DR STRING; 1566270.SAMN03159363_2483; -.
DR OrthoDB; 9761189at2; -.
DR Proteomes; UP000199507; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.90.100.10; Orn/Lys/Arg decarboxylase, C-terminal domain; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005308; OKR_de-COase_N.
DR InterPro; IPR011193; Orn/lys/arg_de-COase.
DR InterPro; IPR000310; Orn/Lys/Arg_deCO2ase_major_dom.
DR InterPro; IPR008286; Prn/Lys/Arg_de-COase_C.
DR InterPro; IPR036633; Prn/Lys/Arg_de-COase_C_sf.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR45229:SF3; BIODEGRADATIVE ARGININE DECARBOXYLASE; 1.
DR PANTHER; PTHR45229; CONSTITUTIVE ORNITHINE DECARBOXYLASE; 1.
DR Pfam; PF01276; OKR_DC_1; 1.
DR Pfam; PF03711; OKR_DC_1_C; 1.
DR Pfam; PF03709; OKR_DC_1_N; 1.
DR PIRSF; PIRSF009393; Orn_decarb; 1.
DR SUPFAM; SSF55904; Ornithine decarboxylase C-terminal domain; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00703; OKR_DC_1; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR009393-1}.
FT DOMAIN 392..406
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|PROSITE:PS00703"
FT MOD_RES 397
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR009393-1"
SQ SEQUENCE 765 AA; 86474 MW; AE9B074468F8C4ED CRC64;
MKFRFPIVII EEDFRYENTS GLGIRALAQA FESEGFEVLG VTSYGDLSQF AQQQSRASAF
ILSIDDEEFT VGPDLDPAVL SLRNFIGEVR RKNADVPIYI YGETKTSRHI PNDILRELHG
FIHMFEDTPE FVARHIIREA KAYLEGVQPP FFKALIDYAE DGSYSWHCPG HSGGVAFLKS
PVGQMFHQFF GENMLRADVC NAVEELGQLL DHTGPVAASE RNAARIFNAD HCFFVTNGTS
TSNKMVWHHT VAPDDVVVVD RNCHKSILHA IIMTGAIPVF MKPTRNHFGI IGPIPKSEFE
QSAIKAKIKA NPLLADVDPN KVKPRVMTLT QSTYDGVIYN TETIKNMLDG YVDTLHFDEA
WLPHAAFHPF YGAYHAMGKR RVRPKESLVF ATQSTHKLLA GISQASHVLV QDSQNRQLDR
DLFNEAYLMH SSTSPQYAII ASCDVAAAMM EPPGGTALVE ESILEALDFR RAMRKVEEEF
GKDEWWFKVW GPEKLVDEGI GRAEDWIMHG EKNRQPKSKK SPRNWHGFGE LADGFNMLDP
IKSTIVTPGL DLEGNFAETG IPASVVTKFL AEHGVIVEKT GLYSFFIMFT IGITKGRWNT
LLTALQQFKD DYARNQPMWR ILPEFCQQHP GYERLGLRDL CQHIHQLYAR YDVARLTTEM
YLSDLTPAMK PSDAFAHIAH RKTERVEIDE LEGRITTSLI TPYPPGIPLL IPGEVFNKKI
VDYLKFSREF NTQCPGFETD IHGLVARIDE TGKKRYYADC VRKAS
//
