ID F3PX65_9BACE Unreviewed; 373 AA.
AC F3PX65;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Putative acetylornithine transaminase {ECO:0000313|EMBL:EGF52144.1};
GN ORFNames=HMPREF9446_03355 {ECO:0000313|EMBL:EGF52144.1};
OS Bacteroides fluxus YIT 12057.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=763034 {ECO:0000313|EMBL:EGF52144.1, ECO:0000313|Proteomes:UP000003416};
RN [1] {ECO:0000313|EMBL:EGF52144.1, ECO:0000313|Proteomes:UP000003416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12057 {ECO:0000313|EMBL:EGF52144.1,
RC ECO:0000313|Proteomes:UP000003416};
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 (FEB-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:EGF52144.1}.
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DR EMBL; AFBN01000096; EGF52144.1; -; Genomic_DNA.
DR RefSeq; WP_009126572.1; NZ_GL882689.1.
DR AlphaFoldDB; F3PX65; -.
DR STRING; 763034.HMPREF9446_03355; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_1_10; -.
DR Proteomes; UP000003416; 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:InterPro.
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 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:UP000003416}.
SQ SEQUENCE 373 AA; 40817 MW; A058B3DBC5A54146 CRC64;
MNLFDVYPLF DINIVKGKGC HVWDENGTEY LDLYGGHAVI SIGHAHPHYV EMISKQVATL
GFYSNSVINK LQQQVAERLG KACGYDDYSL FLINSGAEAN ENALKLSSFY NGRTRVISFS
KAFHGRTSLA VEVTNNPKII APINDCGHVT YLPLNDIEAM KAELAKGDVC AVIIEGIQGV
GGIQLPTDEF MQALRQTCTE HNTVLILDEI QSGYGRSGKF FAHQYNGIKA DIITVAKGIA
NGFPMAGVLI SPMFTPVYGQ LGTTFGGNHL ACSAALAVLD VIEQEDLVEN AAQVGDFLMT
ELKKFPQIKD VRGRGLMIGL EFGEPIKELR LKLLKEQHVF TGVSGTNVLR LLPPLCLSMG
EADTFLERFQ KVL
//
