ID A0A410DMG2_9CLOT Unreviewed; 358 AA.
AC A0A410DMG2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:QAA30255.1};
GN ORFNames=C1I91_00325 {ECO:0000313|EMBL:QAA30255.1};
OS Clostridium manihotivorum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=2320868 {ECO:0000313|EMBL:QAA30255.1, ECO:0000313|Proteomes:UP000286268};
RN [1] {ECO:0000313|EMBL:QAA30255.1, ECO:0000313|Proteomes:UP000286268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT4 {ECO:0000313|EMBL:QAA30255.1,
RC ECO:0000313|Proteomes:UP000286268};
RA Tachaapaikoon C., Sutheeworapong S., Jenjaroenpun P., Wongsurawat T.,
RA Nookeaw I., Cheawchanlertfa P., Kosugi A., Cheevadhanarak S.,
RA Ratanakhanokchai K.;
RT "Genome Sequencing and Assembly of Anaerobacter polyendosporus strain
RT CT4.";
RL Submitted (JAN-2018) 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; CP025746; QAA30255.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A410DMG2; -.
DR KEGG; cmah:C1I91_00325; -.
DR OrthoDB; 389074at2; -.
DR Proteomes; UP000286268; Chromosome.
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:QAA30255.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000286268};
KW Transferase {ECO:0000313|EMBL:QAA30255.1}.
FT DOMAIN 28..275
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 332
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 187
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 358 AA; 40226 MW; FB327E5185DD545A CRC64;
MHKKLFIPGP VEVRPEVLEQ MARPLIGHRG KEASELQRRI SNNLKKLFYT ESEILLSTSS
GSGLMEGAIR SCTLKKAAVF SSGAFGDRWY EMALNNNVPA DKFEVEWGKG IKAEDVEKAL
STGNYDLITI THNETSTGLM NNLEDISKVV KRYPEVVFCV DTVSSAGGTK IEVDKLGIDI
CITSSQKALG LPPGLAVCTF SNKAKERAEK VPFRGTYLDL LALYKYIKKK DYQYPSTPSI
SHMFALDYEL NYIVNEEGIE NRFERHIEMA NIVRAWAKKY FDIFPEEGYW SNTVTNITNT
RGIDISALNK ELGTRGFQIS NGYGKLKDKT FRIAHMADCT VDEINELLTN INDILGFE
//
