ID U2RWB7_LEIAQ Unreviewed; 398 AA.
AC U2RWB7;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Putative succinylornithine transaminase {ECO:0000313|EMBL:ERK73046.1};
GN ORFNames=N136_00591 {ECO:0000313|EMBL:ERK73046.1};
OS Leifsonia aquatica ATCC 14665.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1358026 {ECO:0000313|EMBL:ERK73046.1, ECO:0000313|Proteomes:UP000016605};
RN [1] {ECO:0000313|EMBL:ERK73046.1, ECO:0000313|Proteomes:UP000016605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14665 {ECO:0000313|EMBL:ERK73046.1,
RC ECO:0000313|Proteomes:UP000016605};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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:ERK73046.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AWVQ01000055; ERK73046.1; -; Genomic_DNA.
DR RefSeq; WP_021764103.1; NZ_KI272407.1.
DR AlphaFoldDB; U2RWB7; -.
DR PATRIC; fig|1358026.3.peg.512; -.
DR HOGENOM; CLU_016922_10_1_11; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000016605; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProt.
DR CDD; cd00610; OAT_like; 1.
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; IPR004636; AcOrn/SuccOrn_fam.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00707; argD; 1.
DR PANTHER; PTHR11986:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000016605}.
SQ SEQUENCE 398 AA; 41852 MW; 53212F7EDEFC318F CRC64;
MSELTQGQWK GRFGDAIMRT LATPKLMLAR GEGCRVWDTD GVEYLDFLAG IAVNSLGHAH
PALVEAVSHQ VGTLAHVSNY FSTAPQLELA ERLRTITGAG DQGRVLFGNS GAEANEAAFK
LARLNRGPHG HRTRVLALNN AFHGRTMGSL ALTGKPPMRE AFEPLPGGVE HIDSTIAALE
AAIDDRVAAL FIEPIKGEAG VLDLPAGFLA RARELTEQHG ALLILDEIQT GVGRTGRWFA
YQHEGILPDA VTVAKGIAGG VPIGALVTFG WASDLFTQGQ HGSTFGGNPL ATAAGNAVLG
EIERAGLVEN AARRGEELRA IIRSYDSPLI GDVSGAGLLI GIGLTEGEAH RLSDAALAEG
LIINAPNESS IRLAPPLIVG DAELAEFRER FGRALAAL
//