ID A0A2S8EQT8_9RHOB Unreviewed; 464 AA.
AC A0A2S8EQT8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Aspartate aminotransferase family protein {ECO:0000313|EMBL:PQO22306.1};
GN ORFNames=C2I36_13670 {ECO:0000313|EMBL:PQO22306.1};
OS Rhodobacteraceae bacterium WD3A24.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=2086263 {ECO:0000313|EMBL:PQO22306.1, ECO:0000313|Proteomes:UP000237945};
RN [1] {ECO:0000313|EMBL:PQO22306.1, ECO:0000313|Proteomes:UP000237945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WD3A24 {ECO:0000313|EMBL:PQO22306.1,
RC ECO:0000313|Proteomes:UP000237945};
RA Wang S.;
RT "The draft genome sequence of Pararoseibaca halophilus WD3A24.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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:PQO22306.1}.
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DR EMBL; PUHN01000053; PQO22306.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S8EQT8; -.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000237945; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; 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 PANTHER; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42684:SF3; GAMMA-AMINOBUTYRATE TRANSAMINASE POP2, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:PQO22306.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000237945};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PQO22306.1}.
SQ SEQUENCE 464 AA; 49456 MW; 059BF3A003F82EBB CRC64;
MTAVSDNLPT AALQRLDAAH HMHPFTAGAE LAARGARVIT RADGVWLTDS EGNRILDGMA
GLWCVNVGYG REELAEAAAR QMRALPYYNT FFQTTHVPAI ALAAKLAELA PDDLNHVFFA
GSGSEANETN IRMARHYWAR KGKPGKQIII SRRNAYHGSS MGSASLGGMA GMHAQGGLPI
PGIVHIDQPN WWAEGGEMSP EEFGRARARQ LEETIAALGE DRVAAFIAEP VQGAGGVIIP
PESYWPEIQR ICDAHDILLI ADEVICGFGR TGEWFASQSY RIRPHIVTVA KGLASGYQPI
GGSIVCDAVA EVIGGGEFNH GYTYSGHPVA CAVALENLRL LEEERVVEHV RDTAAPHLAR
AWAGLADHPL VGEAVSRGLL ASLALTPDKG ARAPFAEPGA AGLICRERAF ANNLVMRHVG
DRMVIAPPLV ITPAEIDELI ARARAALDET HAALDARGLM GAAA
//