ID A0A1N7PGP0_9FLAO Unreviewed; 379 AA.
AC A0A1N7PGP0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Acetylornithine aminotransferase {ECO:0000313|EMBL:SIT09690.1};
GN ORFNames=SAMN05421785_106241 {ECO:0000313|EMBL:SIT09690.1};
OS Chryseobacterium gambrini.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=373672 {ECO:0000313|EMBL:SIT09690.1, ECO:0000313|Proteomes:UP000185781};
RN [1] {ECO:0000313|EMBL:SIT09690.1, ECO:0000313|Proteomes:UP000185781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18014 {ECO:0000313|EMBL:SIT09690.1,
RC ECO:0000313|Proteomes:UP000185781};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-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}.
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DR EMBL; FTOV01000006; SIT09690.1; -; Genomic_DNA.
DR RefSeq; WP_076393606.1; NZ_FTOV01000006.1.
DR AlphaFoldDB; A0A1N7PGP0; -.
DR STRING; 373672.SAMN05421785_106241; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000185781; 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: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 Aminotransferase {ECO:0000313|EMBL:SIT09690.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:SIT09690.1}.
SQ SEQUENCE 379 AA; 42387 MW; 5AC50372CB907FF3 CRC64;
MNLFNVYPLF KINPVKAQGS FLWDDKGEKY LDFYGGHAVI SIGHNHPHYQ TQLKNQLDKI
SFYSNSVQNE LQTELAEKLG KLSGLEEYNL FLCNSGAEAN ENALKLASFH NGKNKVLYFS
GSFHGRTSAA VSVTDNPKIV APVNYDERFI KSEWNNIEQL EEVFEKQGNE ISSVIIEGIQ
GVGGIMIPTV EFLTKIKELC EKYDAVLILD EVQSGYGRSG YFFAHQEFGI EADIITTAKG
MGNGFPIGGV LIHPKFQASY GLLGTTFGGN HLACVAAIAV LDVMKDENLI ENAQKMGEYI
ENEIKDFPHI KNIRRKGLMI GIELDRDCSE VRNSILYNHH IFTGNSNDKA VLRILPALNI
KKEETDLFIN ALKEVLENI
//
