ID D5X6S6_THIK1 Unreviewed; 384 AA.
AC D5X6S6;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Aminotransferase class V {ECO:0000313|EMBL:ADG32073.1};
GN OrderedLocusNames=Tint_2732 {ECO:0000313|EMBL:ADG32073.1};
OS Thiomonas intermedia (strain K12) (Thiobacillus intermedius).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX NCBI_TaxID=75379 {ECO:0000313|EMBL:ADG32073.1};
RN [1] {ECO:0000313|EMBL:ADG32073.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 {ECO:0000313|EMBL:ADG32073.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Kerfeld C.A., Cannon G.C.,
RA Heinhorst S., Woyke T.;
RT "Complete sequence of Thiomonas intermedia K12.";
RL Submitted (APR-2010) 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|PIRSR:PIRSR000524-50};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236}.
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DR EMBL; CP002021; ADG32073.1; -; Genomic_DNA.
DR AlphaFoldDB; D5X6S6; -.
DR STRING; 75379.Tint_2732; -.
DR KEGG; tin:Tint_2732; -.
DR eggNOG; COG0075; Bacteria.
DR HOGENOM; CLU_044792_0_0_4; -.
DR BioCyc; TINT75379:TINT_RS13675-MONOMER; -.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ADG32073.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Transferase {ECO:0000313|EMBL:ADG32073.1}.
FT DOMAIN 21..250
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 384 AA; 41629 MW; 3928F46AF430C1EE CRC64;
MPALLPNVDP DGLLEYSVVY TDRSLNHMSA KFQQVMRDLS SMLKQAYNAQ AAVIVPGSGT
FAMEAVARQF VQGAQVLIVR NGWFSYRWSQ IIETGHLSDK VTVLKARRVA DSSESPFTPA
PIAEVVATIA REKPAVVFAP HVETSAGMML PDDYLRAVAD AVHAVGGVFV LDCIASGAMW
VDMQATGVDV LVSAPQKGWS GQPCCGFAML SERALQRLET TTSDSFSCDL KKWHQIMQAY
EKGTHAYHAT MPTDTLAEVR DQMREAFSYG LPALKAAQIE LGRAARSSLE QRGVKSVAAP
GFQAPGVVVS YTRDPDIQNG KKFVAQGMQI AAGVPLACDE PADYMSFRLG LFGLDKWKDV
PAAVQRLDAA LDAVGLHLPE KAHR
//
