ID A0A081G376_9GAMM Unreviewed; 453 AA.
AC A0A081G376;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000313|EMBL:KEA65231.1};
DE EC=2.6.1.62 {ECO:0000313|EMBL:KEA65231.1};
GN ORFNames=ADIMK_0553 {ECO:0000313|EMBL:KEA65231.1};
OS Marinobacterium lacunae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinobacterium.
OX NCBI_TaxID=1232683 {ECO:0000313|EMBL:KEA65231.1, ECO:0000313|Proteomes:UP000028252};
RN [1] {ECO:0000313|EMBL:KEA65231.1, ECO:0000313|Proteomes:UP000028252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK27 {ECO:0000313|EMBL:KEA65231.1,
RC ECO:0000313|Proteomes:UP000028252};
RA Singh A., Pinnaka A.K.;
RT "Marinobacterium kochiensis sp. nov., isolated from sediment sample
RT collected from Kochi backwaters in Kerala, India.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEA65231.1}.
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DR EMBL; JMQN01000012; KEA65231.1; -; Genomic_DNA.
DR RefSeq; WP_051692372.1; NZ_JMQN01000012.1.
DR AlphaFoldDB; A0A081G376; -.
DR STRING; 1232683.ADIMK_0553; -.
DR PATRIC; fig|1232683.4.peg.545; -.
DR eggNOG; COG0161; Bacteria.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000028252; Unassembled WGS sequence.
DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase 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; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KEA65231.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000028252};
KW Transferase {ECO:0000313|EMBL:KEA65231.1}.
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 49082 MW; D8826CACFE3DCB41 CRC64;
MQSTPKNKKT GTQSFWNPMA HPGDPASRNF IQIVKGDGNY VQTAAGDWLV DGVGGLWNVN
VGHNRQEVKD AINAQLDELE YFQIFDGCSH PRVHELADKL IEMTQPEGMT KAMFSSGGSD
AVETALKIAR QYWKAVGQSQ RYKFISLKQG YHGVHFGGAS VNGNTVFRTS YEPMLPGCIH
IDTPWLYRNP WNCEDPEQLG QLCAAQLEAE IIFQGPETVA AFIAEPVQGA GGVIVPPANY
WPLVRQVCDK YGVLLIADEV VTGFGRSGNM FGVRGWGVKA DIQCFAKGIN SGYIPLGATL
VNERISSAIE GCQSFTGAVM HGYTYSGHPV ACAAALASLK IVEQENLPQN AAVQGELLKT
KLEQALLDFP AVGEIRGKGL MIAIDLVTNK ETREPIDPTN GYANRVAAVA MREGAIVRPV
GTKIILSPTL TLTETEVDKL TSALKIAFQE VKA
//