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Database: UniProt
Entry: A9MPH4_SALAR
LinkDB: A9MPH4_SALAR
Original site: A9MPH4_SALAR 
ID   A9MPH4_SALAR            Unreviewed;       713 AA.
AC   A9MPH4;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Orn/Lys/Arg decarboxylases family 1 pyridoxal-P attachment site domain-containing protein {ECO:0000259|PROSITE:PS00703};
GN   OrderedLocusNames=SARI_02768 {ECO:0000313|EMBL:ABX22617.1};
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514 {ECO:0000313|EMBL:ABX22617.1, ECO:0000313|Proteomes:UP000002084};
RN   [1] {ECO:0000313|EMBL:ABX22617.1, ECO:0000313|Proteomes:UP000002084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980
RC   {ECO:0000313|Proteomes:UP000002084};
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) 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}.
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DR   EMBL; CP000880; ABX22617.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9MPH4; -.
DR   STRING; 41514.SARI_02768; -.
DR   KEGG; ses:SARI_02768; -.
DR   HOGENOM; CLU_014292_3_0_6; -.
DR   Proteomes; UP000002084; Chromosome.
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   CDD; cd00615; Orn_deC_like; 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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR009393-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002084}.
FT   DOMAIN          362..376
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS00703"
FT   MOD_RES         367
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009393-1"
SQ   SEQUENCE   713 AA;  80709 MW;  FB659B3D1CFF9221 CRC64;
     MNIIAIMGPR GVYYKDEPIK ELERALQSLG FQIIWPQNSV DLLKFIEHNP RICGVIFDWD
     EYSLDLCSDI NQLNEYLPLY AFINTNSTLD VSVHDMRMAL WFFEYALGQA EDIATRIHQY
     TNEYLDNITP PFTKALFTYA KEGKYTFCTP GHMAGTAYQK SPAGCLFYDF FGGNTLKADV
     SISVTELGSL LDHTGPHLEA EEYIARTFGA EQSYMVTNGT STSNKIVGMY AAPAGSTLLI
     DRNCHKSLAH LLMMSDVVPL WLKPTRNALG ILGGIPKREF TRDSIARKVA ETAQAQWPVH
     AVITNSTYDG LLYNTNWLKQ MLDVPSIHFD SAWVPYTHFH PIYQGKSGMS GERVPGKVIF
     ETQSTHKMLA AFSQASLIHI KGEYDEETFN EAFMMHTSTS PSYPIVASIE TAAAMLRGNA
     GRRLINRSVE RALHFRKEVR RLREESDSWF FDIWQPEEVD EAECWPVAQG ETWHGFTDAD
     DDHMFLDPVK VTILTPGMDE QGNMSEEGIP AALVAKFLDE RGVVVEKTGP YNLLFLFSIG
     IDKTRAMGLM RGLTEFKRAY DLNLRVKNML PDLYAEDPDF YRNMRIQDLA QGIHKLIRQH
     DLPGLMLRAF DVLPEMIMTP HQAWQRQIKG EVETVALDQL PGRVSANMIL PYPPGVPLLM
     PGERISKESR AVLDFLQMLC SIGQHYPGFE TDIHGAKQNE DGVYQVRVLK HAC
//
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