ID G7ZD91_AZOL4 Unreviewed; 458 AA.
AC G7ZD91;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Putative acetylornithine transaminase {ECO:0000313|EMBL:CBS89373.1};
DE EC=2.6.1.11 {ECO:0000313|EMBL:CBS89373.1};
GN OrderedLocusNames=AZOLI_p20205 {ECO:0000313|EMBL:CBS89373.1};
OS Azospirillum lipoferum (strain 4B).
OG Plasmid AZO_p2 {ECO:0000313|EMBL:CBS89373.1,
OG ECO:0000313|Proteomes:UP000005667}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS89373.1, ECO:0000313|Proteomes:UP000005667};
RN [1] {ECO:0000313|Proteomes:UP000005667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RC PLASMID=Plasmid AZO_p2 {ECO:0000313|Proteomes:UP000005667};
RX PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA Zhulin I.B.;
RT "Azospirillum genomes reveal transition of bacteria from aquatic to
RT terrestrial environments.";
RL PLoS Genet. 7:E1002430-E1002430(2011).
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR EMBL; FQ311870; CBS89373.1; -; Genomic_DNA.
DR AlphaFoldDB; G7ZD91; -.
DR KEGG; ali:AZOLI_p20205; -.
DR HOGENOM; CLU_016922_4_0_5; -.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000005667; Plasmid AZO_p2.
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; PTHR43094; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43094:SF1; 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.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:CBS89373.1};
KW Plasmid {ECO:0000313|EMBL:CBS89373.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:CBS89373.1}.
SQ SEQUENCE 458 AA; 47880 MW; 2A225ACB1A9EDD06 CRC64;
MSANPQPDRS EGDINLGPRR AGWMAGALGP RSRALVERDA AAFLRQSLST PCLSAIRKAE
GIWIEDMDGR RFMDFHGNSV HHIGYAHPRL VAALKAQMDE LSFAPRRFAC EPAAELAERL
TAIAPTGPGS RVLFAPGGSE GIEIALKLAR VATGRFKTVS FWDAFHGAGF GSSSVGGEAL
FRSNGIGPLL AGTEHVAPFA CARCPYGFDP APGGGPDLDT CRMTCARMLR YVLEKEGDVA
AVVAEPVRAV PYVPPPGFWA EVRRACDDAG ALLIFDEIPT GLGKTGSLFS HEPFGARPDI
LVLGKALGGA MLPLAAVIAR AGLDVAADRA LGHYTHEKNP LLARAGLTTL DIVRDEGLAE
RAATLGTLAL ERLRELTGPL PGIADIRGAG LLIGIELADH LGRSAADRAE AAFYAALAAG
VSLKISQGTV LTLSPPLTIA EAELERALAI VAAAIGSA
//
