ID G9ZLY8_9LACO Unreviewed; 457 AA.
AC G9ZLY8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Putative 4-aminobutyrate transaminase {ECO:0000313|EMBL:EHM00072.1};
GN ORFNames=HMPREF9103_00736 {ECO:0000313|EMBL:EHM00072.1};
OS Lentilactobacillus parafarraginis F0439.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=797515 {ECO:0000313|EMBL:EHM00072.1, ECO:0000313|Proteomes:UP000004625};
RN [1] {ECO:0000313|EMBL:EHM00072.1, ECO:0000313|Proteomes:UP000004625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0439 {ECO:0000313|EMBL:EHM00072.1,
RC ECO:0000313|Proteomes:UP000004625};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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:EHM00072.1}.
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DR EMBL; AGEY01000030; EHM00072.1; -; Genomic_DNA.
DR RefSeq; WP_008211349.1; NZ_JH414927.1.
DR AlphaFoldDB; G9ZLY8; -.
DR STRING; 797515.HMPREF9103_00736; -.
DR PATRIC; fig|797515.3.peg.684; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_9; -.
DR Proteomes; UP000004625; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}.
SQ SEQUENCE 457 AA; 49495 MW; 0865B5C3FDC12B63 CRC64;
MLETDELQAS LPQVAMPLPG PEAKKILDKR TENVPSAVLC NYPVVINRGS GAMIEDVDGN
RFLDWVAGVG VMNVGYGQQR VIDAVKKQAD KFFHGMINIT THRNYVDLAA RINELAPVNA
DKKKTMFVNS GAEAVENAVK IAKSFTGRGD VIVFSGAFHG RTALTSTMTA KKTYSYGIEP
AMGGIHRAEF PYLYRAPKGY SRDEAIQYYL DKLQYVFEQG VPAKQVAAIV IEPIQGEGGF
IPAPFEYVKA LRKICDENGI MLVADEVQTG FARSGKLFVS NYWKENGFAP DIIAMAKSIG
AGLPLAAVTA GANIMEGVQP GIVGSTFGGN ALACAAGLQV LDIIHDEKLT DRALNIGKIA
SDGFKDLQSR YDVIGDVRGI GSMIGVEFVK DQTTKEPYPE LVSKLIKHAV SHGLIMENAG
VHDNVIRFLS PLVVTEEQIH AGLKIYEQSL NEALAEL
//
