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Database: UniProt
Entry: A0A3M8H7M4_9BACI
LinkDB: A0A3M8H7M4_9BACI
Original site: A0A3M8H7M4_9BACI 
ID   A0A3M8H7M4_9BACI        Unreviewed;       489 AA.
AC   A0A3M8H7M4;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme {ECO:0000313|EMBL:RNC98387.1};
GN   ORFNames=EC501_11120 {ECO:0000313|EMBL:RNC98387.1};
OS   Lysinibacillus halotolerans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=1368476 {ECO:0000313|EMBL:RNC98387.1, ECO:0000313|Proteomes:UP000279909};
RN   [1] {ECO:0000313|EMBL:RNC98387.1, ECO:0000313|Proteomes:UP000279909}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCCC 1A12703 {ECO:0000313|EMBL:RNC98387.1,
RC   ECO:0000313|Proteomes:UP000279909};
RX   PubMed=24814335; DOI=10.1099/ijs.0.061465-0;
RA   Kong D., Wang Y., Zhao B., Li Y., Song J., Zhai Y., Zhang C., Wang H.,
RA   Chen X., Zhao B., Ruan Z.;
RT   "Lysinibacillus halotolerans sp. nov., isolated from saline-alkaline
RT   soil.";
RL   Int. J. Syst. Evol. Microbiol. 64:2593-2598(2014).
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:RNC98387.1}.
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DR   EMBL; RHLQ01000026; RNC98387.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M8H7M4; -.
DR   OrthoDB; 9815233at2; -.
DR   Proteomes; UP000279909; Unassembled WGS sequence.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00615; Orn_deC_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
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   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43277; ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43277:SF4; ARGININE 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:RNC98387.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000279909};
KW   Transferase {ECO:0000313|EMBL:RNC98387.1}.
FT   DOMAIN          221..235
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS00703"
SQ   SEQUENCE   489 AA;  53631 MW;  61795E35D3AB3EA4 CRC64;
     MSQLETPLFD VLLKHRNRHP IQFHIPGHKK GQGMDPAFRE FVGDNVLSID LINIAPLDDL
     HSPKGAIKEA QKLAAEAFGA DHTFFSVQGT SGAIMAMILT VVGPGDKILV PRNVHKSTMS
     AIVLAGAIPI FIHPEVDEEY GIAHGISAES VEKALKTYPD AKAMLVINPT YFGFAADLKR
     IVDIVHAHNI PVIVDEAHGV HIKFHDELPI SAMQAGADMA ATSVHKLGGS MTQSSVLNVK
     EGLVSVNRVQ SVLSMLTTTS TSYPILASLD CARRQLAVHG YDLIDETIRL AKDARKRINK
     IPHLKVAGRE KLHSSATFDM DITKILISVK DLGITGHQAE EWLRLNANIE VELSDLYNIL
     CLVTLGDTKK EINLLVNALQ RMSLAFESDA SVKETNVNIP DIPALAMTPR DAFYSSTEVM
     PLEESVGYIC AEFIMVYPPG IPIFIPGEII TEDNIRYIQM NIEAGLPVQG PEDLSLKTIR
     VIKERKPIF
//
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