ID A9D2D7_HOEPD Unreviewed; 442 AA.
AC A9D2D7;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000313|EMBL:EDQ34185.1};
DE EC=2.6.1.18 {ECO:0000313|EMBL:EDQ34185.1};
GN ORFNames=HPDFL43_14347 {ECO:0000313|EMBL:EDQ34185.1};
OS Hoeflea phototrophica (strain DSM 17068 / NCIMB 14078 / DFL-43).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Hoeflea.
OX NCBI_TaxID=411684 {ECO:0000313|EMBL:EDQ34185.1, ECO:0000313|Proteomes:UP000004291};
RN [1] {ECO:0000313|EMBL:EDQ34185.1, ECO:0000313|Proteomes:UP000004291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DFL-43 {ECO:0000313|EMBL:EDQ34185.1,
RC ECO:0000313|Proteomes:UP000004291};
RA Wagner-Dobler I., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDQ34185.1, ECO:0000313|Proteomes:UP000004291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DFL-43 {ECO:0000313|EMBL:EDQ34185.1,
RC ECO:0000313|Proteomes:UP000004291};
RA Fiebig A.;
RL Submitted (JUN-2012) 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:EDQ34185.1}.
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DR EMBL; ABIA03000004; EDQ34185.1; -; Genomic_DNA.
DR RefSeq; WP_007198631.1; NZ_CM002917.1.
DR AlphaFoldDB; A9D2D7; -.
DR STRING; 411684.HPDFL43_14347; -.
DR eggNOG; COG0161; Bacteria.
DR HOGENOM; CLU_016922_4_3_5; -.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000004291; Chromosome.
DR GO; GO:0016223; F:beta-alanine-pyruvate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
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; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42684:SF1; BETA-ALANINE--PYRUVATE AMINOTRANSFERASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:EDQ34185.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000004291};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EDQ34185.1}.
SQ SEQUENCE 442 AA; 48213 MW; 2321EAA302D90C90 CRC64;
MSNRLNTTPN DLRAFWMPFT ANRQFKQNPR MMVAAKDMHF SAADGRQVLD GTAGLWCVNA
GHCRPLITEA IRQQVGELDY APAFQMGHPK AFELANRLID IAPDNMANVL FTNSGSESVE
TALKVALAYH RVKGDGSRTR LIGRERGYHG VNFGGISVGG IVANRKMFGT LLTGVDHMPH
THLPEQNAFT RGEPEHGGDL ADELQRIVTL HDPSTIAAVI VEPVAGSTGV LVPPKGYLKR
LREICTQHGI LLIFDEVITG YGRLGSAFAS QHFDVKPDII VTAKGLTNGV IPMGAVFVTQ
EIHDAFMQGP EHMIEFFHGY TYSGNPIACA AALGTLETYK QEGLFERAAE LAPYWEDALH
SLKGEPHVID IRNIGLVGAI ELQGVAGEPT KRAFACFVRA WEKGCLIRTT GDIIALSPPL
IISKSQIDEL IDCVRTVLNE VA
//
