ID A0A3M8EEA1_9BACT Unreviewed; 374 AA.
AC A0A3M8EEA1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Aspartate aminotransferase family protein {ECO:0000313|EMBL:RNC63676.1};
GN ORFNames=D7D25_15325 {ECO:0000313|EMBL:RNC63676.1};
OS Proteiniphilum sp. X52.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC Proteiniphilum.
OX NCBI_TaxID=2382159 {ECO:0000313|EMBL:RNC63676.1, ECO:0000313|Proteomes:UP000272792};
RN [1] {ECO:0000313|EMBL:RNC63676.1, ECO:0000313|Proteomes:UP000272792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X52 {ECO:0000313|EMBL:RNC63676.1,
RC ECO:0000313|Proteomes:UP000272792};
RA Hivarkar S., Lanjekar V.B., Dhakephalkar P.K., Dagar S.;
RL Submitted (OCT-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 -!- 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:RNC63676.1}.
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DR EMBL; RDSD01000025; RNC63676.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8EEA1; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000272792; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009102; P:biotin biosynthetic process; 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:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 3.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Aminotransferase {ECO:0000313|EMBL:RNC63676.1};
KW Biotin biosynthesis {ECO:0000256|ARBA:ARBA00022756};
KW Iron {ECO:0000256|ARBA:ARBA00022714};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022714};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:RNC63676.1}.
SQ SEQUENCE 374 AA; 40401 MW; 80396FEE5D316A96 CRC64;
MNLFDVYSLW EIEPIRAQGC HVWDSEGTKY LDLYGGHAVI SIGHSHPHYV KAVQDQIEKI
GFYSNSVQNS LQQELADKLA EQSGYADYSL FLCNSGAEAN ENALKLASFH TGKKRVIAFH
GAFHGRTSGA VAVTENPAIQ APFNTGHEVT FVPLNDMEAV KAEILKGDVA AVIIEGILGV
AGIFTPETSF LQQLALLCSQ NNVILILDEI QSGYGRSGQF FAHQSAGIRP DLITMAKGMG
NGFPIGGLLI SPQFEAKKGI LGTTFGGNHL ACAAAIAVLD VLKAESLVEN AAYMGDYLKQ
ELSEINGIAE IRGRGLMLGV EFLPECGAVR DRLLYESHIF TGGAKNNVMR LLPSLSISKA
EIDTFITELK DKLI
//
