ID Q2KWF0_BORA1 Unreviewed; 792 AA.
AC Q2KWF0;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Biodegradative arginine decarboxylase {ECO:0000313|EMBL:CAJ50298.1};
DE EC=4.1.1.19 {ECO:0000313|EMBL:CAJ50298.1};
GN Name=adiA {ECO:0000313|EMBL:CAJ50298.1};
GN OrderedLocusNames=BAV2687 {ECO:0000313|EMBL:CAJ50298.1};
OS Bordetella avium (strain 197N).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ50298.1, ECO:0000313|Proteomes:UP000001977};
RN [1] {ECO:0000313|EMBL:CAJ50298.1, ECO:0000313|Proteomes:UP000001977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N {ECO:0000313|EMBL:CAJ50298.1,
RC ECO:0000313|Proteomes:UP000001977};
RX PubMed=16885469; DOI=10.1128/JB.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC {ECO:0000256|ARBA:ARBA00010671}.
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DR EMBL; AM167904; CAJ50298.1; -; Genomic_DNA.
DR RefSeq; WP_012418330.1; NC_010645.1.
DR AlphaFoldDB; Q2KWF0; -.
DR STRING; 360910.BAV2687; -.
DR GeneID; 41394523; -.
DR KEGG; bav:BAV2687; -.
DR eggNOG; COG1982; Bacteria.
DR HOGENOM; CLU_014292_3_0_4; -.
DR OrthoDB; 9761189at2; -.
DR Proteomes; UP000001977; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:CAJ50298.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR009393-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001977}.
FT DOMAIN 22..137
FT /note="Orn/Lys/Arg decarboxylase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03709"
FT DOMAIN 143..598
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|Pfam:PF01276"
FT DOMAIN 624..753
FT /note="Orn/Lys/Arg decarboxylase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03711"
FT REGION 770..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 389
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR009393-1"
SQ SEQUENCE 792 AA; 88058 MW; 560FA12C63DED1DC CRC64;
MKFNHHVLFV LSSALVDDQP AAESIAALQA SLVQRGFQIQ TAGSIKAALS YIEQSPRYSA
IALYWDSGNE NIDTEGEALL QKVRERNAKV PVFLMSQADV SAGVPIGVLK SVSEYIYLYS
ETPAFTANRI YTAVHRYAEK LLPPYFKTLK DFTEDGDYYW DCPGHMGGMA YLKHPVGIEF
INFFGENIMR ADIGVATAEM GDYLIHAGPS KASEEIAAEL FGADWTFYGV AGSSGSNRIV
AQGAIGANEI AVVDRNCHKS LNHGLTLSQA RPVYLTPSRN GYGLIGPIPT HRLKKQSVDA
LIANSPLAPQ AVSKEPTYAV VTNCTYDGFC YKVSDVVKHL GASVPRIHFD EAWYAYAKFH
PLYKDRFAMD IADDMPNRPT IFAVQSTHKM LPALSMASMI HVKKSDRAPL SFDDFNDSFM
MHGTTSPFYP IIASIDVAVS MMQGEAGRSL VQESIEEAVA FRQAVVNVKR QLAEQEGDGS
WFFDVLQPTE AKDPVSGKTY PFHQAPMALL SQTPDVWRLH ENDYWHGFSK EDLRETDCML
DPVKVSITCP GITPDGHYQK GGIPGYIVTK FLDDRRIEVA RTGDYTLLIL FSVGITKGKW
GTLIESLLEF KKLYDNGALA VDAIPSLKTA SSQYDKLTLK ELCTQMHETM HELDLMNHIA
KAVQSTPKPV YTPAEAYQKV VRYKTEPVRV TEFAGRIAAS MLVPYPPGIP VLMPGEQLPT
DDTGIIGYLE ALQEFDKKYP GFEHEIQGVS VDQHGDHWVR AIIEEDREPK KLPEHIKFKR
HTTSTSIKKG RQ
//
