ID K0K4Z1_SACES Unreviewed; 803 AA.
AC K0K4Z1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Biodegradative arginine decarboxylase {ECO:0000313|EMBL:CCH32647.1};
DE EC=4.1.1.19 {ECO:0000313|EMBL:CCH32647.1};
GN Name=adiA {ECO:0000313|EMBL:CCH32647.1};
GN OrderedLocusNames=BN6_53880 {ECO:0000313|EMBL:CCH32647.1};
OS Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC
OS 15066 / NRRL 15764).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH32647.1, ECO:0000313|Proteomes:UP000006281};
RN [1] {ECO:0000313|EMBL:CCH32647.1, ECO:0000313|Proteomes:UP000006281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764
RC {ECO:0000313|Proteomes:UP000006281};
RX PubMed=22958348; DOI=10.1186/1471-2164-13-465;
RA Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J.,
RA Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.;
RT "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and
RT comparison to the other completely sequenced Pseudonocardiaceae.";
RL BMC Genomics 13:465-465(2012).
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC {ECO:0000256|ARBA:ARBA00010671}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE804045; CCH32647.1; -; Genomic_DNA.
DR AlphaFoldDB; K0K4Z1; -.
DR STRING; 1179773.BN6_53880; -.
DR KEGG; sesp:BN6_53880; -.
DR PATRIC; fig|1179773.3.peg.5428; -.
DR eggNOG; COG1982; Bacteria.
DR HOGENOM; CLU_014292_3_0_11; -.
DR OrthoDB; 9815233at2; -.
DR BioCyc; SESP1179773:BN6_RS26050-MONOMER; -.
DR Proteomes; UP000006281; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
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 Lyase {ECO:0000313|EMBL:CCH32647.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR009393-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006281}.
FT DOMAIN 423..437
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|PROSITE:PS00703"
FT MOD_RES 428
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR009393-1"
SQ SEQUENCE 803 AA; 87882 MW; 709A16E24FD8D9DE CRC64;
MRAIHVSVTK PLYVPPLITL ERNSGEGAER VTESTILIVT EKSAADNTVP AAKVEQVCAH
LRECGHEVMV VHSTTDAASA VTSQADLAAA VMSWELVGGA LQSADTDPAV PGGVLRMLLD
RFSSRLPVFL LTTGEYDDET PLWVSEVING WIWLLEDTPD FIAGRVDFAA HQYLDQVLPP
FFRELRRFDD THPYSWHTPA HAGGIAFLKS PVGRAFYDYY GERLFRTDIS VSVGELGSLF
EHTGPVGEAE RNAARIFGAD ETYFVLHGTS SSNRMIVHSA VANDEITLLD RNCHKAINHG
VILTGARPVY LVPTRNGYGI TGPIPPERLT ADAVRAQVER TPIAAGAVSP DPAYAVITNS
TYDGLCYDAV RVNELLGAST RTLHFDEAWF AYGRFNPLYA RRYGMAVDGD GLPDAQRPTV
FTTHSSHKLL AALSQSAMIH VKSGSKAPFD PTRFNETYMM HGTTSPLYPM IASCDVAAGM
MDGPAGNWLT SEAITEAVRF RQAMVRLGRR LADAGDRPPW FFGVWQPGEV TDAGTGERVE
FHRAPLDLLR TDPRCWTLEP DAEWHGFPGL EPGFCMLDPV KVTITCPGVD ALGGVSAFGV
PARVVTAYLE TRRIVVEKTD VYTFLVLFSM GITKGKWGTL LDALTDFKQL HDDNAPLPEV
LPDLVKAHPE RYGRLTLPQL CEEMHDSLAA SKVVQLLNEA FTSPTPPTAV MTPAEAYQHF
IRGETELVGL AELADRVVAT QVTTTPPGIP VLVPGERVGP PDGPLLRYLR VLEAFDQRFP
GFANETHGVH HEGGKYWISC VTE
//
