ID M4NBJ0_9GAMM Unreviewed; 439 AA.
AC M4NBJ0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000313|EMBL:AGG87964.1};
GN ORFNames=R2APBS1_0799 {ECO:0000313|EMBL:AGG87964.1};
OS Rhodanobacter denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=666685 {ECO:0000313|EMBL:AGG87964.1, ECO:0000313|Proteomes:UP000011859};
RN [1] {ECO:0000313|EMBL:AGG87964.1, ECO:0000313|Proteomes:UP000011859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2APBS1 {ECO:0000313|EMBL:AGG87964.1,
RC ECO:0000313|Proteomes:UP000011859};
RG US DOE Joint Genome Institute;
RA Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA Munk A.C.C., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E.,
RA Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Peters L., Pitluck S., Woyke T., Prakash O., Elkins J., Brown S.,
RA Palumbo A., Hemme C., Zhou J., Watson D., Jardine P., Kostka J., Green S.;
RT "Complete genome of Rhodanobacter sp. 2APBS1.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR EMBL; CP003470; AGG87964.1; -; Genomic_DNA.
DR RefSeq; WP_015446957.1; NZ_CP088918.1.
DR AlphaFoldDB; M4NBJ0; -.
DR STRING; 666685.R2APBS1_0799; -.
DR KEGG; rhd:R2APBS1_0799; -.
DR eggNOG; COG0161; Bacteria.
DR HOGENOM; CLU_016922_4_0_6; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000011859; 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; PTHR43094; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
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:AGG87964.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:AGG87964.1}.
SQ SEQUENCE 439 AA; 46658 MW; 72B0306FEEDB8F26 CRC64;
MANERDSVLH SWCVQAAWQA PTVVGGRGAY LELEDGRRIL DMSSLAECSN LGHQHPAVVA
AIREQAQQLC FVTSAWGAQP RAELAEALLE KAGFDGGRVF FTLAGADANE NAVKFARQAS
GKPRGHIVTR DRSYHGASYA CMALSGDART RSQVDPEAFG VLHVPPPDTY RCPFGSEDAQ
ACGEHAVAAV AQAIDHQGAS SVAAVLMEPN AGTNGIVAPD SYWPGLREVT RERGVYLIAD
EVMSGFGRCG EWFAWQRHGD AGKPDLMTLA KGLTGAHLPL GAVVLSAPVA ARLQHEMLYT
GLTYCGHPLS CAAGLAALRA YEDEDLIARS RILGGWMLAE LRALQAHHPV IGDVRGGHGL
FAVVELVENR DTRAPLAPWP QTPPALSALV DAAMAQGVSF ASRGNLLLLA PPLVIENHAL
ADALSLLDRL LAHFFPAVA
//
