ID E6X4I3_CELAD Unreviewed; 374 AA.
AC E6X4I3;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Acetylornithine transaminase {ECO:0000313|EMBL:ADV48283.1};
DE EC=2.6.1.11 {ECO:0000313|EMBL:ADV48283.1};
GN OrderedLocusNames=Celal_0958 {ECO:0000313|EMBL:ADV48283.1};
OS Cellulophaga algicola (strain DSM 14237 / IC166 / ACAM 630).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=688270 {ECO:0000313|EMBL:ADV48283.1, ECO:0000313|Proteomes:UP000008634};
RN [1] {ECO:0000313|EMBL:ADV48283.1, ECO:0000313|Proteomes:UP000008634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14237 / IC166 / ACAM 630
RC {ECO:0000313|Proteomes:UP000008634};
RX PubMed=21475589; DOI=10.4056/sigs.1543845;
RA Abt B., Lu M., Misra M., Han C., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA Pagani I., Ivanova N., Mavromatis K., Ovchinikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Brambilla E., Rohde M., Tindall B.J., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Cellulophaga algicola type strain (IC166).";
RL Stand. Genomic Sci. 4:72-80(2010).
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; CP002453; ADV48283.1; -; Genomic_DNA.
DR RefSeq; WP_013549770.1; NC_014934.1.
DR AlphaFoldDB; E6X4I3; -.
DR STRING; 688270.Celal_0958; -.
DR KEGG; cao:Celal_0958; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_1_10; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000008634; Chromosome.
DR GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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:ADV48283.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:ADV48283.1}.
SQ SEQUENCE 374 AA; 41145 MW; 75BB7007E5B81814 CRC64;
MKLFDVYPLY NVTPVSAKGS IVTDINGQEY WDFYGGHAVI SIGHGHPHYV KRLEDQLHKI
GFYSNAIQNP LQTELATKLG VLSDCEDYNL FLCSSGAEAN ENALKMASFI TGKSRVIAFN
NGFHGRTSAA VAATDNQNIN APINKQQKVT FLPFDAIDAF ESEIKKGDVC AVILEAIQGV
GGLDEPSTEF YQEIARSCKE HGVILIADEV QSGFGRSGKF FGFQHHNIQP DIISIAKGMG
NGFPVGGVLI HESIEAKYGM LGTTFGGNHL ACAASLAVLE VIEKEKLIEN ADKIGNYFKK
RAVEIPQVKK IKGRGLMLGL EFDFEVSELR KRLIYDQHIF TGGASNKKLL RILPALNISE
KEIDIFFEAL KKEL
//
