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Database: UniProt
Entry: U2RWB7_LEIAQ
LinkDB: U2RWB7_LEIAQ
Original site: U2RWB7_LEIAQ 
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}.
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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
//
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