ID A7HVI1_PARL1 Unreviewed; 400 AA.
AC A7HVI1;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN OrderedLocusNames=Plav_2300 {ECO:0000313|EMBL:ABS63914.1};
OS Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Parvibaculaceae; Parvibaculum.
OX NCBI_TaxID=402881 {ECO:0000313|EMBL:ABS63914.1, ECO:0000313|Proteomes:UP000006377};
RN [1] {ECO:0000313|EMBL:ABS63914.1, ECO:0000313|Proteomes:UP000006377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-1 / DSM 13023 / NCIMB 13966
RC {ECO:0000313|Proteomes:UP000006377};
RX PubMed=22675581; DOI=10.4056/sigs.2215005;
RA Schleheck D., Weiss M., Pitluck S., Bruce D., Land M.L., Han S.,
RA Saunders E., Tapia R., Detter C., Brettin T., Han J., Woyke T., Goodwin L.,
RA Pennacchio L., Nolan M., Cook A.M., Kjelleberg S., Thomas T.;
RT "Complete genome sequence of Parvibaculum lavamentivorans type strain (DS-
RT 1(T)).";
RL Stand. Genomic Sci. 5:298-310(2011).
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 ECO:0000256|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC ECO:0000256|RuleBase:RU000481}.
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DR EMBL; CP000774; ABS63914.1; -; Genomic_DNA.
DR RefSeq; WP_012111220.1; NC_009719.1.
DR AlphaFoldDB; A7HVI1; -.
DR STRING; 402881.Plav_2300; -.
DR KEGG; pla:Plav_2300; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_5; -.
DR OrthoDB; 9763453at2; -.
DR Proteomes; UP000006377; Chromosome.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:RHEA.
DR GO; GO:0030170; F:pyridoxal phosphate binding; 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; IPR004838; NHTrfase_class1_PyrdxlP-BS.
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.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW ECO:0000313|EMBL:ABS63914.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006377};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:ABS63914.1}.
FT DOMAIN 32..392
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 400 AA; 43592 MW; 0F15E6DE91B509CB CRC64;
MGFISDALNR IQPSATIAAT QKARDLKALG RDVISLAAGE PDFDTPDNIK EAAIKAIREG
KTKYTAVDGI PELKAAICAK FKRENGLDYQ PNQAFVAPGG KPIIYNAMIA TLNPGDEVII
PAPYWVSYPD IVLLAGGTPV TVDTTLKNGF KLQPEELEKA ITKKTKWLIF NSPSNPSGAA
YTHDELKKLT DVLMKHPQVW ILSDDMYEHL TYDGFKFATP AEVEPGLYER TLTMNGVSKA
YAMTGWRIGY CAGPEPLIKA MTKVQSQSTS NPTSISQWAA VEALNGPQDF IPTRAASFKE
RRDLVVSMLN QAKGIKCPTP EGAFYVYPSC EGCIGKETTV GKVIESDEDF ALALLEAEGV
SVVHGAAFGL SPFFRISYAT STEELTDACE RIQRFCASLR
//
