ID R6QKE1_9FIRM Unreviewed; 386 AA.
AC R6QKE1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Acetylornithine aminotransferase {ECO:0000313|EMBL:CDC33459.1};
GN ORFNames=BN563_01498 {ECO:0000313|EMBL:CDC33459.1};
OS Eubacterium sp. CAG:251.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1262886 {ECO:0000313|EMBL:CDC33459.1, ECO:0000313|Proteomes:UP000018414};
RN [1] {ECO:0000313|EMBL:CDC33459.1, ECO:0000313|Proteomes:UP000018414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:251 {ECO:0000313|Proteomes:UP000018414};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDC33459.1}.
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DR EMBL; CBFD010000077; CDC33459.1; -; Genomic_DNA.
DR AlphaFoldDB; R6QKE1; -.
DR STRING; 1262886.BN563_01498; -.
DR Proteomes; UP000018414; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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 Aminotransferase {ECO:0000313|EMBL:CDC33459.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000018414};
KW Transferase {ECO:0000313|EMBL:CDC33459.1}.
SQ SEQUENCE 386 AA; 42101 MW; 33948CEE238EF78B CRC64;
METKELDNDY VAHAYGRFNV TLNNGKGSTI SDDNGKQYID FGSGIGVTAF GICDDEWKAA
VETQLDKMQH VSNLYYTEPC ARLAKMLCDK TGMKKVFFGN SGAEANEGAI KFARKYSYDK
YGEGRSTIIT LVNSFHGRTI TTLAATGQDS FHTVFGPFTP GFKYCPANDI EKLNEMATDD
VCAIMFECVQ GEGGVNNLDY NFVKAIEKLA KEKDILMVVD EVQTGNGRTG KYFAYENFDI
KPDIVSTAKG LAGGLPMGAV LFGEKVKDTV TPGSHGSTFG GNPVCAAGAI SIVSRIDDEF
LKSVREKSEY IKNFLMNIKG VKSVSGMGLM LGVETQKDAK QIASECLENG LLVLTAKTKI
RLLPALNISY LELDRGLKIL KEVIEK
//
