ID C7N0Z1_SLAHD Unreviewed; 402 AA.
AC C7N0Z1;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE SubName: Full=Ornithine/acetylornithine aminotransferase {ECO:0000313|EMBL:ACV23213.1};
DE EC=2.6.1.11 {ECO:0000313|EMBL:ACV23213.1};
GN OrderedLocusNames=Shel_22030 {ECO:0000313|EMBL:ACV23213.1};
OS Slackia heliotrinireducens (strain ATCC 29202 / DSM 20476 / NCTC 11029 /
OS RHS 1) (Peptococcus heliotrinreducens).
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Slackia.
OX NCBI_TaxID=471855 {ECO:0000313|EMBL:ACV23213.1, ECO:0000313|Proteomes:UP000002026};
RN [1] {ECO:0000313|EMBL:ACV23213.1, ECO:0000313|Proteomes:UP000002026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29202 / DSM 20476 / NCTC 11029 / RHS 1
RC {ECO:0000313|Proteomes:UP000002026};
RX PubMed=21304663; DOI=10.4056/sigs.37633;
RA Pukall R., Lapidus A., Nolan M., Copeland A., Glavina Del Rio T., Lucas S.,
RA Chen F., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L., Kuske C.,
RA Brettin T., Detter J.C., Han C., Pitluck S., Pati A., Mavrommatis K.,
RA Ivanova N., Ovchinnikova G., Chen A., Palaniappan K., Schneider S.,
RA Rohde M., Chain P., D'haeseleer P., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Kyrpides N.C., Klenk H.P., Hugenholtz P.;
RT "Complete genome sequence of Slackia heliotrinireducens type strain (RHS
RT 1).";
RL Stand. Genomic Sci. 1:234-241(2009).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001684; ACV23213.1; -; Genomic_DNA.
DR RefSeq; WP_012799313.1; NC_013165.1.
DR AlphaFoldDB; C7N0Z1; -.
DR STRING; 471855.Shel_22030; -.
DR KEGG; shi:Shel_22030; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_1_11; -.
DR OMA; GHYWSGI; -.
DR Proteomes; UP000002026; 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; 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:ACV23213.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000002026};
KW Transferase {ECO:0000313|EMBL:ACV23213.1}.
SQ SEQUENCE 402 AA; 43013 MW; 5BA6DFC077C1E356 CRC64;
MTLEHEQQLE NEYVMPTFVR KPVEFVSGSG MELVDDKGKT YLDFIGGIGV IAIGHCNPVL
ADALAEQAHK LMHVSNYYYV EGRGDLSKKL CDMLNHGAAE PEVWKTFYTN SGAESNECAV
KIARLHAKKN GRGGTIVTLE GSFHGRTLAT LAATAQPAKQ EAFQPLPAGF VATPPNDVAA
LEALFEAQGT DIAAVLVEPI QGEGGVKPLT QEFMQAVREQ CTKHGALMMC DEVQTGIYRC
GTPYAFQKFG VVPDVVSMAK GIGGGMPMGA CAARGEIADT FSPGDHGTTF GGSCLAITAA
NTTLDYIQEH DIAANIEETG AYLREQLATL PHMKEVRGMG LMDAIEFDDT VDAPALVLAA
LEADQGLVLN YTGPHTMRFL PPLVCTKADV DVMIAQMKEL LG
//