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Database: UniProt
Entry: A0A081G376_9GAMM
LinkDB: A0A081G376_9GAMM
Original site: A0A081G376_9GAMM 
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
//
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