ID   A0A3D8Z1R2_9BACL        Unreviewed;       482 AA.
AC   A0A3D8Z1R2;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme {ECO:0000313|EMBL:REB11457.1};
GN   ORFNames=DVB69_00645 {ECO:0000313|EMBL:REB11457.1};
OS   Sporosarcina sp. BI001-red.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX   NCBI_TaxID=2282866 {ECO:0000313|EMBL:REB11457.1, ECO:0000313|Proteomes:UP000256461};
RN   [1] {ECO:0000313|EMBL:REB11457.1, ECO:0000313|Proteomes:UP000256461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BI001-red {ECO:0000313|EMBL:REB11457.1,
RC   ECO:0000313|Proteomes:UP000256461};
RA   Rajandas H., Sivachandran P., Mai C.W., Cheong K.W., Teh C.S.J.,
RA   Lim E.S.H., Yap I.K.S., Convey P., Chong C.W.;
RT   "Draft Genome of Sporosarcina subantarcticus.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:REB11457.1}.
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DR   EMBL; QQAK01000002; REB11457.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8Z1R2; -.
DR   OrthoDB; 9815233at2; -.
DR   Proteomes; UP000256461; Unassembled WGS sequence.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.105.10; Molybdopterin biosynthesis moea protein, domain 2; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
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   PANTHER; PTHR43277; ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43277:SF3; LYSINE DECARBOXYLASE; 1.
DR   Pfam; PF01276; OKR_DC_1; 1.
DR   Pfam; PF03711; OKR_DC_1_C; 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   Aminotransferase {ECO:0000313|EMBL:REB11457.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000256461};
KW   Transferase {ECO:0000313|EMBL:REB11457.1}.
FT   DOMAIN          219..233
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS00703"
SQ   SEQUENCE   482 AA;  52586 MW;  EE5A5114BA54A3FC CRC64;
     MDHTKRPVVE ALQTFLAARP VSFHVPGHKH GLLSRLPQDL KAALRYDVTE LTGLDDLHAP
     TEMLAEAQTM LADVYGADRS FFLVNGSTVG NIAMIRTVCA PGDTLLVQRN AHKSVFHALE
     LAAVQAVLLT PEWDEATCTA GAVSSATVEE ALERYPDAKG VVVTYPTYYG TTGSDLPMIV
     EKVHKRGIPV LVDEAHGAHF VAGTPFPTSA LRLGADIVVQ SAHKTLSAMT QASFLHVNSQ
     LIDIERLARI LSMLQTSSPS YVLLASLDDA RAMIATYSAD DKQAFLIWRG EFIDQLRKIK
     ALEVIETEDP LKILIRQQEA SGYTLQHSLE EKGIYTELAD ERQVLLVLPL LTEGTSYPTQ
     SICEAVESAV QLLKRDSVRV PLKDETNEEE PRELIITTSS LSKKNTDWVS AESASGYQAA
     AAIIPYPPGI PLVLSGEQLN LQQIQEVCEM MESGAKFQGS VRANGPTVEF EVLRAQGEDG
     ND
//