ID H0QW72_9ACTN Unreviewed; 492 AA.
AC H0QW72;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Putative lyase {ECO:0000313|EMBL:GAB17073.1};
GN ORFNames=GOEFS_018_01050 {ECO:0000313|EMBL:GAB17073.1};
OS Gordonia effusa NBRC 100432.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1077974 {ECO:0000313|EMBL:GAB17073.1, ECO:0000313|Proteomes:UP000035034};
RN [1] {ECO:0000313|EMBL:GAB17073.1, ECO:0000313|Proteomes:UP000035034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100432 {ECO:0000313|EMBL:GAB17073.1,
RC ECO:0000313|Proteomes:UP000035034};
RA Yoshida I., Takarada H., Hosoyama A., Tsuchikane K., Katsumata H.,
RA Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia effusa NBRC 100432.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family. Sphingosine-
CC 1-phosphate lyase subfamily. {ECO:0000256|ARBA:ARBA00038302}.
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:GAB17073.1}.
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DR EMBL; BAEH01000018; GAB17073.1; -; Genomic_DNA.
DR RefSeq; WP_007316411.1; NZ_BAEH01000018.1.
DR AlphaFoldDB; H0QW72; -.
DR STRING; 1077974.GOEFS_018_01050; -.
DR eggNOG; COG0076; Bacteria.
DR OrthoDB; 3401800at2; -.
DR Proteomes; UP000035034; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR42735; -; 1.
DR PANTHER; PTHR42735:SF6; SPHINGOSINE-1-PHOSPHATE LYASE 1; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000035034}.
FT MOD_RES 234
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 492 AA; 51403 MW; 8158C4626790B114 CRC64;
MTDDSRATRI LGRLEALREA DAPTHGGRVL SYVYDSGLTE LDDLAAAVTR LVQPVNGLDP
TVFTSVAAME REVIAFGRTI FHGDQTVGTV TSGGTESCVL AVKAARDHAG VVAGSGAIVV
PSTAHAAFDK AAKLLGVQII RVPVDVVTTA VTVDAVASAL RDDTFLIVAS APNYPTGTAD
PIVELGQLAV ERELPLHVDA CLGGFALAWW PDESLAPWDF RVPGVSSLSA DLHKYGYTPK
GASLLLHADR DRHRAQYFAT TDWPGYPVVN PTLLGSRSVA GLAASWAIIE YLGEDGFGDL
VARVADSSRQ LISAVESIDG LRVVGEPVGP VFAVASDPTS GTVVDTHRWS QAVTRRGFAL
QVQPRYPQAD GTVLPPTTHL TITPVTERIV DELVDVFVEA ADEVRGLPPQ SPPQALADLA
ELLANGSLDV DAVLGLPSEA TAAALVAAGV DPHGAGSSEL DMPAIVAAVQ ALPRSVTAKM
LAEFLASFTN PA
//
