ID A0A142LYM1_AMIAI Unreviewed; 323 AA.
AC A0A142LYM1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Ornithine cyclodeaminase {ECO:0000313|EMBL:MBB3707023.1};
DE EC=4.3.1.12 {ECO:0000313|EMBL:MBB3707023.1};
GN ORFNames=FHS67_003350 {ECO:0000313|EMBL:MBB3707023.1};
OS Aminobacter aminovorans (Chelatobacter heintzii).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Aminobacter.
OX NCBI_TaxID=83263 {ECO:0000313|EMBL:MBB3707023.1, ECO:0000313|Proteomes:UP000577697};
RN [1] {ECO:0000313|EMBL:MBB3707023.1, ECO:0000313|Proteomes:UP000577697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10368 {ECO:0000313|EMBL:MBB3707023.1,
RC ECO:0000313|Proteomes:UP000577697};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ornithine cyclodeaminase/mu-crystallin
CC family. {ECO:0000256|ARBA:ARBA00008903}.
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:MBB3707023.1}.
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DR EMBL; JACICB010000011; MBB3707023.1; -; Genomic_DNA.
DR RefSeq; WP_067954874.1; NZ_JACICB010000011.1.
DR AlphaFoldDB; A0A142LYM1; -.
DR STRING; 83263.AA2016_0250; -.
DR OrthoDB; 9785971at2; -.
DR Proteomes; UP000577697; Unassembled WGS sequence.
DR GO; GO:0008473; F:ornithine cyclodeaminase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.1780.10; ornithine cyclodeaminase, domain 1; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003462; ODC_Mu_crystall.
DR InterPro; IPR023401; ODC_N.
DR PANTHER; PTHR13812; KETIMINE REDUCTASE MU-CRYSTALLIN; 1.
DR PANTHER; PTHR13812:SF19; KETIMINE REDUCTASE MU-CRYSTALLIN; 1.
DR Pfam; PF02423; OCD_Mu_crystall; 1.
DR PIRSF; PIRSF001439; CryM; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:MBB3707023.1}.
SQ SEQUENCE 323 AA; 34009 MW; 4ECD226047CB9969 CRC64;
MLHFSADDID RALTFPGLVE TLRTAFREGA VQPVRHHHTV ERAKGTDSTL LLMPAWTDFK
AAGAGADGHI GVKIVTVSPD NNDIAKPAVV GLYLLLDGIT GEPQALMDGP RLTQWRTACA
SALAASYLAR EDASKLLVIG AGAQCRFLAR AHAAVRPIKE IRVWNRTPAN AETLAASLRD
EGFEATAVSD LDAELGWADI ITAGTISTTP LVKGARLKPG AHVDLVGGFT PGMREADDDA
IAKARVYVDT RAGATKEAGD IVQPIAAGVL TADAIVADLH ELARDQKPAR QSADEITLFK
SVGAALEDLA AGIAVYESLK PKA
//
