ID W8VS87_9FLAO Unreviewed; 393 AA.
AC W8VS87;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Acetylornithine aminotransferase {ECO:0000313|EMBL:BAO56719.1};
GN ORFNames=NMS_2710 {ECO:0000313|EMBL:BAO56719.1};
OS Nonlabens marinus S1-08.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Nonlabens.
OX NCBI_TaxID=1454201 {ECO:0000313|EMBL:BAO56719.1, ECO:0000313|Proteomes:UP000031760};
RN [1] {ECO:0000313|EMBL:BAO56719.1, ECO:0000313|Proteomes:UP000031760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S1-08 {ECO:0000313|EMBL:BAO56719.1,
RC ECO:0000313|Proteomes:UP000031760};
RX PubMed=24706784; DOI=10.1073/pnas.1403051111;
RA Yoshizawa S., Kumagai Y., Kim H., Ogura Y., Hayashi T., Iwasaki W.,
RA DeLong E.F., Kogure K.;
RT "Functional characterization of flavobacteria rhodopsins reveals a unique
RT class of light-driven chloride pump in bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:6732-6737(2014).
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; AP014548; BAO56719.1; -; Genomic_DNA.
DR RefSeq; WP_041497223.1; NZ_AP014548.1.
DR AlphaFoldDB; W8VS87; -.
DR STRING; 1454201.NMS_2710; -.
DR HOGENOM; CLU_016922_10_1_10; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000031760; 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; 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:BAO56719.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:BAO56719.1}.
SQ SEQUENCE 393 AA; 43384 MW; 484EB6CE5A4A6DDC CRC64;
MKKDFFTYQA PTTPYAPGLE IARAEGSYIY DINGNSYLDM VAGVSALPLG HCHPKVTQAI
KAQVDQYMHV MVYGEYAQAP AVELCKKIAS TLPEPLRMTY LVNSGTEAIE ASIKLARTVT
KRREIIAMHH SYHGNTMGSL SLMDYEERKA PFRPLLPDIS HIKFNCIPDL RRISNKTAAV
ILETIQGAAG FILPHPEWLK QLRKICDQLG VLIILDEIQP GVGRTGTMWH FQNYDFIPDM
VVSGKGLGGG LPIGALTASV AHLSHFKSAP MLGHITTFGG NPVIASAALA TLNAIEEESL
MDAVKLKEAR FRESLNSSNI KQVRGKGLML AAILPDDKHT AAIVDECRNR GVIFFLLLFE
KRAIRITPPY TVTMEEIDKA CTILCDVVDE FYP
//
