ID A0A095XW63_9GAMM Unreviewed; 396 AA.
AC A0A095XW63;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Aspartate aminotransferase {ECO:0000313|EMBL:KGE03936.1};
DE EC=2.6.1.1 {ECO:0000313|EMBL:KGE03936.1};
GN ORFNames=HRUBRA_01441 {ECO:0000313|EMBL:KGE03936.1};
OS Pseudohaliea rubra DSM 19751.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Pseudohaliea.
OX NCBI_TaxID=1265313 {ECO:0000313|EMBL:KGE03936.1, ECO:0000313|Proteomes:UP000029640};
RN [1] {ECO:0000313|EMBL:KGE03936.1, ECO:0000313|Proteomes:UP000029640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19751 {ECO:0000313|EMBL:KGE03936.1,
RC ECO:0000313|Proteomes:UP000029640};
RX PubMed=25414506;
RA Spring S., Fiebig A., Riedel T., Goker M., Klenk H.P.;
RT "Genome Sequence of Gammaproteobacterial Pseudohaliea rubra Type Strain DSM
RT 19751, Isolated from Coastal Seawater of the Mediterranean Sea.";
RL Genome Announc. 2:e01208-14(2014).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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:KGE03936.1}.
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DR EMBL; AUVB01000042; KGE03936.1; -; Genomic_DNA.
DR RefSeq; WP_035514844.1; NZ_KN234751.1.
DR AlphaFoldDB; A0A095XW63; -.
DR STRING; 1265313.HRUBRA_01441; -.
DR PATRIC; fig|1265313.6.peg.1425; -.
DR eggNOG; COG1448; Bacteria.
DR HOGENOM; CLU_032440_0_1_6; -.
DR OrthoDB; 9766445at2; -.
DR Proteomes; UP000029640; Unassembled WGS sequence.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR000796; Asp_trans.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11879; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR11879:SF22; ASPARTATE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KGE03936.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000029640};
KW Transferase {ECO:0000313|EMBL:KGE03936.1}.
FT DOMAIN 27..391
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 396 AA; 42647 MW; E6A7A774789C86AC CRC64;
MLHTLERLPD DPILGLAAAC RADPNPDKVD LTVGIYMDED GVCPVFGAIR DAQRALVEEE
TSKAYLPPAG DPDFNTGMRA LVFGGDSGAL ADGRVSSLAA PGGCGALRIG AEIARVASPE
AKVWVSDPTW PVHMPLIGSV GLEFEKYRYY DAPSHGVDFD GMVEDLKRAK SGDLVLLHGC
CHNPCGADLT LEQWGVIAEL AERQGFLPFI DIAYQGLGDG LEADAAGLRL LAERLPEMIV
AASCSKNMGL YRERTGIAQF LCRDAGNAEA ILSQAKVAAR RIYSMPPAHG ALLAGRVLAA
PALEAAWRDE LHTMCLRING LREALVEKLE ATTGRDFAFI RREKGMFSFL GLSEEQTRRL
REEYSVYMLG SSRINVAGIN AANIDYVADA VARVIA
//
