ID J6LI04_9RHOB Unreviewed; 400 AA.
AC J6LI04;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=aspartate transaminase {ECO:0000256|ARBA:ARBA00012753};
DE EC=2.6.1.1 {ECO:0000256|ARBA:ARBA00012753};
GN ORFNames=A33M_1939 {ECO:0000313|EMBL:EJW12523.1};
OS Rhodovulum sp. PH10.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=1187851 {ECO:0000313|EMBL:EJW12523.1, ECO:0000313|Proteomes:UP000002930};
RN [1] {ECO:0000313|EMBL:EJW12523.1, ECO:0000313|Proteomes:UP000002930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PH10 {ECO:0000313|EMBL:EJW12523.1,
RC ECO:0000313|Proteomes:UP000002930};
RX PubMed=23105089; DOI=10.1128/JB.01695-12;
RA Khatri I., Nupur, Korpole S., Subramanian S., Pinnaka A.K.;
RT "Draft Genome Sequence of Rhodovulum sp. Strain PH10, a Phototrophic
RT Alphaproteobacterium Isolated from a Soil Sample of Mangrove of Namkhana,
RT India.";
RL J. Bacteriol. 194:6363-6363(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000984};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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:EJW12523.1}.
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DR EMBL; AKZI01000029; EJW12523.1; -; Genomic_DNA.
DR RefSeq; WP_008384486.1; NZ_AKZI01000029.1.
DR AlphaFoldDB; J6LI04; -.
DR STRING; 1187851.A33M_1939; -.
DR PATRIC; fig|1187851.3.peg.1201; -.
DR eggNOG; COG0436; Bacteria.
DR OrthoDB; 9763453at2; -.
DR Proteomes; UP000002930; 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: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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:EJW12523.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002930};
KW Transferase {ECO:0000313|EMBL:EJW12523.1}.
FT DOMAIN 32..392
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 400 AA; 42759 MW; 25DEB91579852526 CRC64;
MAFLADSLAR IKPSATIAVA DKARALKAAG RDVIGLGSGE PDFDTPDTIK EAAIKAIRDG
KTKYTNVDGI PELKAAIAAK FERENGLTYK PAEISVGTGG KQVLYNAFVA TLNPGDEVII
PAPYWVSYPE MVLLAGGTPV SVPTTQESGF KLTPEVLERA ITPKTKWLLL NSPSNPSGAA
YTRAELNALT DVVLRHPHVW VMTDDMYEHL VYDGFAFTTP AQVEPGIFDR TLTVNGVSKA
YCMTGWRIGF AGGPTPLIKA MAVVQSQSTS NPNSIAQWAS VEALNGPQDF IAAHNEVFKQ
RRDLVVSMLN QAKGIDCPVP EGAFYVFPSC AGTIGKTAPT GNTIATDDDF VTELLEAEGV
AVVQGSAFGH GPNFRISYAA STDTLKAACE RIQRFCANLR
//
