ID F2NAQ4_CORGP Unreviewed; 427 AA.
AC F2NAQ4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Acetylornithine aminotransferase apoenzyme {ECO:0000313|EMBL:AEB07510.1};
DE EC=2.6.1.11 {ECO:0000313|EMBL:AEB07510.1};
GN OrderedLocusNames=Corgl_1409 {ECO:0000313|EMBL:AEB07510.1};
OS Coriobacterium glomerans (strain ATCC 49209 / DSM 20642 / JCM 10262 / PW2).
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC Coriobacteriaceae; Coriobacterium.
OX NCBI_TaxID=700015 {ECO:0000313|EMBL:AEB07510.1, ECO:0000313|Proteomes:UP000006851};
RN [1] {ECO:0000313|Proteomes:UP000006851}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 49209 / DSM 20642 / JCM 10262 / PW2
RC {ECO:0000313|Proteomes:UP000006851};
RX PubMed=23961308; DOI=10.4056/sigs.3507020;
RA Stackebrandt E., Zeytun A., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S., Liolios K.,
RA Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Huntemann M., Pati A.,
RA Chen A., Palaniappan K., Chang Y.J., Land M., Hauser L., Rohde M.,
RA Pukall R., Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Coriobacterium glomerans type strain (PW2(T))
RT from the midgut of Pyrrhocoris apterus L. (red soldier bug).";
RL Stand. Genomic Sci. 8:15-25(2013).
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; CP002628; AEB07510.1; -; Genomic_DNA.
DR RefSeq; WP_013709252.1; NC_015389.1.
DR AlphaFoldDB; F2NAQ4; -.
DR STRING; 700015.Corgl_1409; -.
DR KEGG; cgo:Corgl_1409; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_1_11; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000006851; 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; 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:AEB07510.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000006851};
KW Transferase {ECO:0000313|EMBL:AEB07510.1}.
SQ SEQUENCE 427 AA; 45134 MW; 82A48BCEBDA9762A CRC64;
MSLDQEQTLE ASYMMQTFAR LDVEFTRGEG MSLEGDDGRR YLDFLAGIGV CCLGYAHPAL
TAAIEAQAHR LLHVSNFFFI EHRGEVAAML SKLANGDALG ARALARAIKS QDGEAVAAAS
APRAGEQIWQ TFFANSGAEA NETSMKLARL FARRKGNKGN TIICLRGSFH GRTHETLAAT
MQDHLQEPFK PLPDGFIACE PNSIEQLQAI FGEQGSEICA VMVEAIQGES GVHPLTQDFM
RAARDLVHSH GGLLISDEVQ TGLFRTGAPF ASHLFGIHPD IMSLAKGIAG GVPMGACVAR
REVAEAFEPG DHGSTFGGSP LSVAAAEAVL SELVVGRFGE RVSEVGAYMA EQLAALSHVV
EVRGAGLMIG CDIDEASGDA RDVVARALEA GFVLSATGPR TLRFLPPLIC TKTDVGALVA
GLADVLG
//
