ID A0A0C1N2V7_9CYAN Unreviewed; 511 AA.
AC A0A0C1N2V7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Arginine decarboxylase {ECO:0000313|EMBL:KIE06766.1};
GN ORFNames=DA73_0236380 {ECO:0000313|EMBL:KIE06766.1};
OS Tolypothrix bouteillei VB521301.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE06766.1};
RN [1] {ECO:0000313|EMBL:KIE06766.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KIE06766.1};
RX PubMed=25700407;
RA Chandrababunaidu M.M., Singh D., Sen D., Bhan S., Das S., Gupta A.,
RA Adhikary S.P., Tripathy S.;
RT "Draft Genome Sequence of Tolypothrix boutellei Strain VB521301.";
RL Genome Announc. 3:e00001-15(2015).
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:KIE06766.1}.
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DR EMBL; JHEG02000059; KIE06766.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C1N2V7; -.
DR STRING; 1479485.DA73_0236380; -.
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}.
FT DOMAIN 238..252
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|PROSITE:PS00703"
SQ SEQUENCE 511 AA; 55097 MW; 740580463EDCD1A9 CRC64;
MTLDANDIFL KTYLPAMLDQ NQTPLLDTLK ACAERPHAPF YTPGHKRGQG ISPLLTDVFG
QSVFRADLPE LAELDNLFSP NGVIHQAQQL AADAFGASQT WFLVNGSTCG IEAAILATCE
ADDKIILPRN VHSSAIAGLI LSGAIPIFVY PEYDAVLDLA HGITPNAVHA ALKKHPDAKA
VLMVYPTYYG VCGDVRAIAS LAHQHNIPLL VDEAHGAHFA FHPQLPTPAL AAGADLTVQS
IHKVLGAMTQ ASMLHIQGNR IDPDRVSKAL QLVQSTSPSY ILLASLDAAR QQMALHGKEL
MSRTLELAEN ARNRISQIPG FSVLEISPNP AFQGAIALDK TRLTVTISGL GVTGFEAEEI
LNDKLGVTAE LASLQHLTFI ISLGNTQEDI EKLVQAFTIL STKINSRVWQ IGSDIDSFSM
RSELTSLNNS LCLSPRKAFF AATETLPLKE TTERICAEIV CPYPPGIPVL MPGEVITKTA
LDYLQYIQRT GGFISGCADS SLNTLKVVKS H
//
