ID A0A172XQG1_9FLAO Unreviewed; 379 AA.
AC A0A172XQG1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Acetylornithine aminotransferase {ECO:0000313|EMBL:ANF49191.1};
GN ORFNames=A0O34_00850 {ECO:0000313|EMBL:ANF49191.1};
OS Chryseobacterium glaciei.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1685010 {ECO:0000313|EMBL:ANF49191.1, ECO:0000313|Proteomes:UP000077824};
RN [1] {ECO:0000313|EMBL:ANF49191.1, ECO:0000313|Proteomes:UP000077824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IHBB 10212 {ECO:0000313|EMBL:ANF49191.1,
RC ECO:0000313|Proteomes:UP000077824};
RA Pal M., Swarnkar M.K., Kaushal K., Chhibber S., Singh A.K., Gulati A.;
RT "Complete Genome Sequence of Chryseobacterium sp. IHBB 10212.";
RL Submitted (APR-2016) 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; CP015199; ANF49191.1; -; Genomic_DNA.
DR RefSeq; WP_066750178.1; NZ_CP015199.1.
DR AlphaFoldDB; A0A172XQG1; -.
DR STRING; 1685010.A0O34_00850; -.
DR KEGG; chh:A0O34_00850; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000077824; Chromosome.
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; 2.
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:ANF49191.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:ANF49191.1}.
SQ SEQUENCE 379 AA; 42172 MW; D985CD5DE8B25C91 CRC64;
MNLFNVYPLF NINPVKAQGS FLWDDKGEKY LDFYGGHAVI SIGHNHPHYQ TQLKNQLDKI
SFYSNSVQNE LQTELADKLG KLSGLEDYNL FLCNSGAEAN ENALKLASFH NGKSKVLYFS
GSFHGRTSAA VSVTDNPKIV APVNYDERFI KSEWNNIEQL EAIFEKQGNE ISSVIIEGIQ
GVGGIMIPTV EFLTKIKELC EKHDTVLILD EVQSGYGRSG YFFAYQEFGI EADIITTAKG
MGNGFPIGGV LIHPKFQASN GLLGTTFGGN HLACVAAIAV LDVMKDENLI ENAQKMGAYI
ENEIKDFPHI KTIRRKGLMI GIELDRDCSE VRNNLLYNHH IFTGNSNDKS VLRILPALNI
KKEETDLFIS ALKTVLENL
//