ID A0A1E4I664_9PROT Unreviewed; 747 AA.
AC A0A1E4I664;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Lysine decarboxylase {ECO:0000313|EMBL:ODU04874.1};
GN ORFNames=ABS89_03020 {ECO:0000313|EMBL:ODU04874.1};
OS Thiobacillus sp. SCN 63-1177.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=1660147 {ECO:0000313|EMBL:ODU04874.1, ECO:0000313|Proteomes:UP000094540};
RN [1] {ECO:0000313|EMBL:ODU04874.1, ECO:0000313|Proteomes:UP000094540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
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:ODU04874.1}.
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DR EMBL; MEFI01000035; ODU04874.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4I664; -.
DR Proteomes; UP000094540; 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 390..404
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|PROSITE:PS00703"
FT MOD_RES 395
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR009393-1"
SQ SEQUENCE 747 AA; 84364 MW; EDF3664DBB1EB6EB CRC64;
MRFRFPIVII DEDFRSENAS GLGIRTLAEA IEKEGMEVLG VTNYGDLTSF AQQQARASAF
VLSIDDEELA GSAEDANNAL QKLRGFVEEV RFRNAEIPIF LHGETRTARH IPNDILRELN
GFIHMLEDTP EFLARYIGRE ARAYLDSLVP PFFRALTHYA ADGSYSWHCP GHSGGVAFLK
SPIGQMFHQF FGENLLRADV CNAVDELGQL LDHTGPVGAS ERNAARIFNC DHLFFVTNGT
SSSNKMVWHA TVAPGDIVVV DRNCHKSILH AIMMCGAIPI FLTPTRNHYG IIGPIPLDEF
RPENIEKKIA AHPFAKDVKR KPRILTITQS TYDGILYNVD MIKELLGDYI DTLHFDEAWL
PHATFHDFYR GMHAIGKNRP RAKDALVFAT QSTHKLLAGL SQASQILVQD SETRKLDFHR
FNEAYLMHTS TSPQYAIIAS CDVAAAMMEP PGGPALVEES IREALDFRRA MRKVDEEFGD
SWWFKVWGPQ KLAEEDVGDR EDWMLETGAR WHEFGKIAPG FNMLDPIKAT VITPGLDVDG
AFADWGIPAA IVTKYLAEHG VIVEKTGLYS FFIMFTIGIT KGRWNTLVTA LQQFKADYDE
NQPLWRVLPE FIEKHPRYEK TGLKDLCDQI HTIYKAKDVA RLTTEMYLSE MAPAMKPADA
FAKMAHREIE RVEIDKLEGR ITAMLVTPYP PGIPLLIPGE RFNGTIVRYL QFTREFNEKF
PGFETDVHGL VEDVVDGKPR YYVDCVI
//
