ID J1F469_9LACO Unreviewed; 456 AA.
AC J1F469;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Class III aminotransferase {ECO:0000313|EMBL:KRN10171.1};
GN ORFNames=FD00_GL000406 {ECO:0000313|EMBL:KRN10171.1};
OS Liquorilactobacillus mali KCTC 3596 = DSM 20444.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1046596 {ECO:0000313|EMBL:KRN10171.1, ECO:0000313|Proteomes:UP000050898};
RN [1] {ECO:0000313|EMBL:KRN10171.1, ECO:0000313|Proteomes:UP000050898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20444 {ECO:0000313|EMBL:KRN10171.1,
RC ECO:0000313|Proteomes:UP000050898};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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:KRN10171.1}.
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DR EMBL; AYYH01000013; KRN10171.1; -; Genomic_DNA.
DR RefSeq; WP_003688450.1; NZ_BACP01000058.1.
DR AlphaFoldDB; J1F469; -.
DR PATRIC; fig|1046596.6.peg.428; -.
DR OrthoDB; 9807885at2; -.
DR Proteomes; UP000050898; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KRN10171.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:KRN10171.1}.
SQ SEQUENCE 456 AA; 49622 MW; DBABB80D1FEB76AB CRC64;
MLSTKLPKII TKQLPGPKAN IILSERKKYV PNSVGCIYPV VIENSEGAII QDPDGNLFLD
WVGGVGVLNV GHTNPRVVEA VKKQSEKYLH GMFNIVTHKG YTKLAQKLAE IAPVKKNEEV
KVFFANSGAE VNENAIKIAK VYTKRPNVIV FSGAFHGRTL LTMTMTSKKA YAKGTGPLAD
GIFRADFPNL YHLPKGIKEE DAIEYYLARI NQIFEEESAA DQVAAIVLEP VQGEGGFIPA
PLKWVEAVRK ICDENGILLI ADEVQSGFAR TGRMFASNYW QEAGFTPDIL TVAKSIAGGL
PLGGVIARKE IMDSVPKGVI GGTFGGNAVA CAAALEVLEI IKDEDLITKA QKIGTRCKKE
FLEWKTKYPV IGDVRGWGAM LGIEFVEDKK TKEPATKFVS DLIQLCVSKG LIIENAGAHG
NVIRFLAPLV ITEDQLNVGL TILEESIQEL SVSKIS
//
