ID K2B8S4_9BACT Unreviewed; 714 AA.
AC K2B8S4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Orn/Lys/Arg decarboxylases family 1 pyridoxal-P attachment site domain-containing protein {ECO:0000259|PROSITE:PS00703};
GN ORFNames=ACD_42C00614G0001 {ECO:0000313|EMBL:EKD76785.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD76785.1};
RN [1] {ECO:0000313|EMBL:EKD76785.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
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:EKD76785.1}.
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DR EMBL; AMFJ01017885; EKD76785.1; -; Genomic_DNA.
DR AlphaFoldDB; K2B8S4; -.
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}.
FT DOMAIN 364..378
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|PROSITE:PS00703"
FT MOD_RES 369
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR009393-1"
SQ SEQUENCE 714 AA; 81894 MW; FAC79B625A0944FD CRC64;
MHNIIFIYPE NIHADQLTYF HELQEKLIKN KFEVLVEHNY HNVIDTVIVN TRIVCVIFDW
EHCPLEILEK FADYKPNLPI IAISTRHKDV DLDLKEFSLN LDFLQFDIAL SDQGLYRIKQ
HIDDYKKNIL PPFTRQLMEF VKKNDYAFCT PGHQAGLGFQ KTPVGTYFYD FYGPNIFRSD
ISISMPEMGS LLEHSGPHKE AEEYIADTFN ADRSLMVTNG TSTANKIVGM YLVSDGDTIL
VDRNCHKSLT HLMMMVDAHP IYMKPTRNAY GIIGGIPASE FSRDIIQKKL DTHPTTKSWP
VYAVITNSTY DGIFYNVDQI KSTLDVKHIH FDSAWVPYTN FHPIYKGKYG MCGDATPEKT
IYETQSTHKL LAAFSQASMI HIKGKFDETR LNESFMMHTT TSPFYPIVAA CEVSAAMMRG
RVGYHVINDT ISCAIDFRNE ITKLHKECDS WFYQVWQPSD IKKVEAWPLN PNDQWHGFSN
VDKNHLYLDP IKVTILLPGM KNGEMEETGI PASVVSAFLE DHGIVVEKTG PYVMLFLFSL
GVTRAKSMRL IAVLNKFKTL YDENATVKEV LPTIYAQDPI FYADMCIQTL AQKQHVLMRQ
YNLPDLLYHA FDQLPKFVMT PHQAYQRLVR NKIKIIPLDD LLNEISAVMV LPYPPGIPLI
MPGESVTPET KVILEYLKLL EMIGKQCPGF EIEIHGLEPG KDGRLYIRVI DEKK
//
