ID A0A5C6EF88_9BACT Unreviewed; 774 AA.
AC A0A5C6EF88;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 02-APR-2025, entry version 14.
DE SubName: Full=Biodegradative arginine decarboxylase {ECO:0000313|EMBL:TWU46256.1};
DE EC=4.1.1.19 {ECO:0000313|EMBL:TWU46256.1};
GN Name=adiA {ECO:0000313|EMBL:TWU46256.1};
GN ORFNames=Poly51_56520 {ECO:0000313|EMBL:TWU46256.1};
OS Rubripirellula tenax.
OC Bacteria; Pseudomonadati; Planctomycetota; Planctomycetia; Pirellulales;
OC Pirellulaceae; Rubripirellula.
OX NCBI_TaxID=2528015 {ECO:0000313|EMBL:TWU46256.1, ECO:0000313|Proteomes:UP000318288};
RN [1] {ECO:0000313|EMBL:TWU46256.1, ECO:0000313|Proteomes:UP000318288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Poly51 {ECO:0000313|EMBL:TWU46256.1,
RC ECO:0000313|Proteomes:UP000318288};
RA Wiegand S., Jogler M., Boedeker C., Pinto D., Vollmers J., Rivas-Marin E.,
RA Kohn T., Peeters S.H., Heuer A., Rast P., Oberbeckmann S., Bunk B.,
RA Jeske O., Meyerdierks A., Storesund J.E., Kallscheuer N., Luecker S.,
RA Lage O.M., Pohl T., Merkel B.J., Hornburger P., Mueller R.-W., Bruemmer F.,
RA Labrenz M., Spormann A.M., Op Den Camp H., Overmann J., Amann R.,
RA Jetten M.S.M., Mascher T., Medema M.H., Devos D.P., Kaster A.-K.,
RA Ovreas L., Rohde M., Galperin M.Y., Jogler C.;
RT "Deep-cultivation of Planctomycetes and their phenomic and genomic
RT characterization uncovers novel biology.";
RL Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC {ECO:0000256|ARBA:ARBA00010671}.
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:TWU46256.1}.
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DR EMBL; SJPW01000008; TWU46256.1; -; Genomic_DNA.
DR RefSeq; WP_146462007.1; NZ_SJPW01000008.1.
DR AlphaFoldDB; A0A5C6EF88; -.
DR OrthoDB; 9815233at2; -.
DR Proteomes; UP000318288; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:TreeGrafter.
DR GO; GO:0006527; P:arginine catabolic process; IEA:TreeGrafter.
DR FunFam; 3.40.640.10:FF:000008; Lysine decarboxylase, inducible; 1.
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 Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:TWU46256.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR009393-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000318288}.
FT DOMAIN 395..409
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|PROSITE:PS00703"
FT MOD_RES 400
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR009393-1"
SQ SEQUENCE 774 AA; 87166 MW; 3DE885B0E28BA048 CRC64;
MKFRFPILII DEDYRSENTS GLGIRALAEA MEGEGAEVIG ATSYGDLSQF AQQQSRASAF
ILSIDDEEVM SSDEEEGPAI GKLREFIQEI RFKNNDIPIF LYGETRTSAH IPNDILRELH
GFIHMFEDTP EFVARHILRE ARSYTDGLAP PFFRALLDYA RDGSYSWHCP GHSGGVAFLK
SPVGQMFHQF FGENMLRADV CNAVEELGQL LDHTGPVAAS ERNAARIFNA DHCFFVTNGT
STSNKMVWHS TVASGDIVVV DRNCHKSILH SIIMTGAVPV FLTPKRNHFG LIGPIPLEEF
LPENIQKKID ANPFARAVQE ANPGRKPRIL TITQSTYDGI VYNVEMLEEL LDGKIGTLHF
DEAWLPHATF HDFYRNMHAI GRDRPRCEES MVFATHSTHK LLAGISQASQ ILVKEPKNQK
LDRHIFNEAY LMHTSTSPQY AIIASCDVAA AMMEPPGGTA LVEESILEAL NFRRAMRKVD
AEWGDDWWFQ VWGPDEIPEH GIGEQSDWIL KADDEWHGFG HLADGFNMLD PIKGTVITPG
LNLHGQFAET GIPASIVTRY LAEHGVIVEK AGLYSFFIMF TIGITKGRWN TLVSALQQFK
DDYDKNLPMW KILPEFAAKF PKYESVGLRD LSHAIHDTYK QSDIARVTTE MYLSEITPAM
LPYVAYDKMT HREIDRVEID DLLGRVTAVL LTPYPPGIPL LIPGECFNQT IIEYLQFARK
FNERFPGFET DIHGLVTETV NGVRKYHVDC IRTKPDQELE QNTASAVKNL VATN
//