ID A0A172ZC57_9BACL Unreviewed; 583 AA.
AC A0A172ZC57;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Amino acid decarboxylase {ECO:0000313|EMBL:ANF95093.1};
GN ORFNames=AR543_02940 {ECO:0000313|EMBL:ANF95093.1};
OS Paenibacillus bovis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1616788 {ECO:0000313|EMBL:ANF95093.1, ECO:0000313|Proteomes:UP000078148};
RN [1] {ECO:0000313|Proteomes:UP000078148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD3526 {ECO:0000313|Proteomes:UP000078148};
RA Wu Z., Gao C., Liu Z., Zheng H.;
RT "Genome of Paenibacillus bovis sp. nov.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ANF95093.1, ECO:0000313|Proteomes:UP000078148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD3526 {ECO:0000313|EMBL:ANF95093.1,
RC ECO:0000313|Proteomes:UP000078148};
RX PubMed=26769366; DOI=10.1099/ijsem.0.000900;
RA Gao C., Han J., Liu Z., Xu X., Hang F., Wu Z.;
RT "Paenibacillus bovis sp. nov., isolated from raw yak (Bos grunniens)
RT milk.";
RL Int. J. Syst. Evol. Microbiol. 66:1413-1418(2016).
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; CP013023; ANF95093.1; -; Genomic_DNA.
DR RefSeq; WP_060531710.1; NZ_CP013023.1.
DR AlphaFoldDB; A0A172ZC57; -.
DR STRING; 1616788.AR543_02940; -.
DR KEGG; pbv:AR543_02940; -.
DR OrthoDB; 9815233at2; -.
DR Proteomes; UP000078148; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR Gene3D; 3.90.1150.150; -; 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 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000078148}.
FT DOMAIN 27..435
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|Pfam:PF01276"
FT DOMAIN 513..558
FT /note="Orn/Lys/Arg decarboxylase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03711"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 583 AA; 64712 MW; 0DFE7299764FC56D CRC64;
MNHKKNQLSK IESKNGTTNH KQSSTAPLYE KLLQYASSGQ RSFHVPGHKN GAIYQSSAIS
ETFGQDVWEA ILRIDVTEIE GTDDLHHPEE VILEGQQLAA ACFGAEESHW LVGGSTSGNL
ALLLTVCTHP GDIVIVQRNV HKSIIHGLMM AGAKAVFLTP VLEPQSTLAV IPDLQSVQQA
LRQYPDAKAV MLTSPNYYGV GADLTAIAAE CHAHHIPLFI DEAHGAHYGH HSRFPSSALK
AGADGVVQST HKMLAAMTMG AMLHIQGPRI NRTLSKQRLS MLQSSSPSYP IMASLDLSRY
LIDQYGTELF EKGLEARDSF VQGIAESDRF EVLKISCSDA QHRENKQTAI TLNTDTDTDT
DIDIDIDTAR GRLAESSGEK IAHWTQDPFK VVIYDRMNVL SGTELQKLLE QHGCFPEMSD
DRYVVLVFSL GSRMEDTIQA LQALQQIEEQ LVITDSRTQI QEDNRHEAIA ETVFSYSDTL
DEPVDTKRYE SDLHNNRIPL ISEPVEFTMI PVSEEQIEAI SLEQANGRRS AEMIIPYPPG
IPILYPGEYI GEQVHAQLML VRNHHMKVQG AMDTSLNTIR VYI
//
