ID S9ZRD3_9RHOO Unreviewed; 402 AA.
AC S9ZRD3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=M622_02430 {ECO:0000313|EMBL:EPZ16052.1};
OS Thauera terpenica 58Eu.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=1348657 {ECO:0000313|EMBL:EPZ16052.1, ECO:0000313|Proteomes:UP000015455};
RN [1] {ECO:0000313|EMBL:EPZ16052.1, ECO:0000313|Proteomes:UP000015455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=58Eu {ECO:0000313|EMBL:EPZ16052.1,
RC ECO:0000313|Proteomes:UP000015455};
RA Liu B., Frostegard A.H., Shapleigh J.P.;
RT "Draft genome sequence of Thauera terpenica.";
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000481};
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 ECO:0000256|RuleBase:RU000481}.
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:EPZ16052.1}.
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DR EMBL; ATJV01000048; EPZ16052.1; -; Genomic_DNA.
DR RefSeq; WP_021248893.1; NZ_ATJV01000048.1.
DR AlphaFoldDB; S9ZRD3; -.
DR STRING; 1348657.M622_02430; -.
DR PATRIC; fig|1348657.5.peg.1465; -.
DR eggNOG; COG1448; Bacteria.
DR OrthoDB; 9766445at2; -.
DR Proteomes; UP000015455; 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: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; 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; PTHR11879:SF37; AROMATIC-AMINO-ACID AMINOTRANSFERASE; 1.
DR PANTHER; PTHR11879; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
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:EPZ16052.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000015455};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:EPZ16052.1}.
FT DOMAIN 31..396
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 402 AA; 42951 MW; B48AD789B2619C74 CRC64;
MSASIFAAVE MAPRDPILGL NEAFGADTRA EKVNLGVGVY YDDNGKIPLL AAVRTAEKAR
LEAMPPRGYQ PIEGLAAYNS GVQNLLFGKD SELASSGQVV TIEALGGTGA LKVGADYLKR
LLPGASVYIS DPSWENHRAL FESAGFQVNN YAYYDAATRG VNFAGMKASL EAAPAGSIIV
LHACCHNPTG ADLSDAQWDE VVSVCRSRGL VPFLDMAYQG FADGIDADAV AVRAFSASGL
QFFVSSSFSK SFSLYGERVG ALSIVTASKE EAGRVLSQVK RVIRTNYSNP PIHGGAIVAA
VLNSPELRQM WEDELAGMRE RIRAMRTSLV EQLKAEGVAQ DFSFVIAQRG MFSYTGLSAE
QVEKLKADFG IYAVSTGRIC LAALNTRNIS YVAKAIAQVI KS
//
