ID A0A1Y4AVP1_9BACE Unreviewed; 374 AA.
AC A0A1Y4AVP1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Aspartate aminotransferase family protein {ECO:0000313|EMBL:OUO24078.1};
GN ORFNames=B5F91_00275 {ECO:0000313|EMBL:OUO24078.1};
OS Bacteroides sp. An322.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1965632 {ECO:0000313|EMBL:OUO24078.1, ECO:0000313|Proteomes:UP000195527};
RN [1] {ECO:0000313|Proteomes:UP000195527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An322 {ECO:0000313|Proteomes:UP000195527};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUO24078.1}.
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DR EMBL; NFIN01000001; OUO24078.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4AVP1; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000195527; 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:OUO24078.1};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000195527};
KW Transferase {ECO:0000313|EMBL:OUO24078.1}.
SQ SEQUENCE 374 AA; 40942 MW; 9A5F15AB789A37C4 CRC64;
MKLFDVYPLF DINIVKGKGC HVWDDKGEEY LDLYGGHAVI SIGHAHPHYV ETISKQVATL
GFYSNSVINK LQQEVADRLG AMCGYDDYQL FLINSGAEAN ENALKLASFY NGRTRVISFC
KAFHGRTSLA VEVTDNPKII APINANQHVT YLPLNDTEAM KAELAKGDVC AVIIEGIQGV
GGIQVPDTAF MQALRQACDE TNTVLILDEI QSGYGRSGKF FAHQYSGIRP DMITVAKGIG
NGFPMGGVLI SPKFKPVYGQ LGTTFGGNHL ACAAAIAVLD VMKEEHLVEN AAKVGAHLLE
ELKKFKGIKE VRGCGLMIGM EFEEPIKELR RKLLFEQKVF TGVSGTNVIR LLPPLCLSMA
EADEFLTRLQ NVLK
//
