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Database: UniProt
Entry: A0A401ID38_APHSA
LinkDB: A0A401ID38_APHSA
Original site: A0A401ID38_APHSA 
ID   A0A401ID38_APHSA        Unreviewed;       494 AA.
AC   A0A401ID38;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 11.
DE   RecName: Full=Orn/Lys/Arg decarboxylases family 1 pyridoxal-P attachment site domain-containing protein {ECO:0000259|PROSITE:PS00703};
GN   ORFNames=AsFPU1_0491 {ECO:0000313|EMBL:GBF79099.1};
OS   Aphanothece sacrum FPU1.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Aphanothecaceae; Aphanothece.
OX   NCBI_TaxID=1920663 {ECO:0000313|EMBL:GBF79099.1, ECO:0000313|Proteomes:UP000287247};
RN   [1] {ECO:0000313|Proteomes:UP000287247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FPU1 {ECO:0000313|Proteomes:UP000287247};
RA   Kanesaki Y., Yoshikawa S., Ohki K.;
RT   "Physiological properties and genetic analysis related to exopolysaccharide
RT   production of fresh-water unicellular cyanobacterium Aphanothece sacrum,
RT   Suizenji Nori, that has been cultured as a food source in Japan.";
RL   Submitted (MAY-2017) 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:GBF79099.1}.
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DR   EMBL; BDQK01000001; GBF79099.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401ID38; -.
DR   OrthoDB; 9815233at2; -.
DR   Proteomes; UP000287247; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   CDD; cd00615; Orn_deC_like; 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; 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: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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287247}.
FT   DOMAIN          230..244
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS00703"
SQ   SEQUENCE   494 AA;  53321 MW;  8120C2CAB97D1A34 CRC64;
     MKLSQDSVWH SQSITPLIET LRTLSQQSRA AFYAPGHKGG QGIPQPLATL LGATVFRSDL
     PELPELDNLF APSGTIKQAQ TLAAAAFGAD QTWFLVNGST CGIIAAILAT CGTGDKIIVP
     RNTHQSFIAG LILSGAVPVF IKSEYDPLWD LPYSFTPEAL EDALNQNSDV KAVLMVYPTY
     HGICGDIKAI AEITHRHDIP LLVDEAHGAH FAFHPSLPPC ALSMGADLAV QSTHKVLGAM
     TQASMLHIKG SRVNPQRISQ ALQLVQSTSP SYLLLASLDG ARQQMALQGE ELLDNTIKLA
     QKARDEISQI KGLSVLNIDK LGLGFHYLDP TRLTVNVTAL GLSGFEVDEI LHQKLGVTAE
     LPMLSHLAFI VSIGNTQKDI NQLIKAFQTL ANITPSPPHP ITYSYPHPIS HPPLSLSPRD
     AFFALTEMIS IEDSIGRISG ELICPYPPGI PVLMPGEIIT QEAINYLVYI QQLGANITGC
     SDETLNTLKV ILFS
//
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