ID A3SNH3_ROSNI Unreviewed; 433 AA.
AC A3SNH3;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Beta alanine-pyruvate transaminase {ECO:0000313|EMBL:EAP76013.1};
DE EC=2.6.1.18 {ECO:0000313|EMBL:EAP76013.1};
GN ORFNames=ISM_14145 {ECO:0000313|EMBL:EAP76013.1};
OS Roseovarius nubinhibens (strain ATCC BAA-591 / DSM 15170 / ISM).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=89187 {ECO:0000313|EMBL:EAP76013.1, ECO:0000313|Proteomes:UP000005954};
RN [1] {ECO:0000313|EMBL:EAP76013.1, ECO:0000313|Proteomes:UP000005954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-591 / DSM 15170 / ISM
RC {ECO:0000313|Proteomes:UP000005954};
RA Moran M.A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (DEC-2005) 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:EAP76013.1}.
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DR EMBL; AALY01000002; EAP76013.1; -; Genomic_DNA.
DR RefSeq; WP_009814838.1; NZ_CH724156.1.
DR AlphaFoldDB; A3SNH3; -.
DR STRING; 89187.ISM_14145; -.
DR eggNOG; COG0161; Bacteria.
DR HOGENOM; CLU_016922_4_3_5; -.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000005954; Unassembled WGS sequence.
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:EAP76013.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Pyruvate {ECO:0000313|EMBL:EAP76013.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005954};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EAP76013.1}.
SQ SEQUENCE 433 AA; 46585 MW; EC884DFCFD851E38 CRC64;
MNDASPIPND LDSFWMPFTS SRAFKAAPRL VSGAKGLYYT TVDGREVFDG TGGLWCSNAG
HGHPRIIEAI QKQAAEMDFA HCFGQGHPIA FQAASRMVAL APGFDHVFFT NSGSESVDTA
LKIALGYHSA RGEGQRRILV GRQKAYHGIN FGGLSVGGIG LNKGQFGTLY PSAQHLRHTN
LPENRMSKGQ PETGAHLAED LAMICETHGG HNVAAVIVEP VAGAGGVFPP PKGYLERLRE
ICDQHGILLI FDEVITGFGR MGTPFASQHF GVKPDIFTAA KGMTNATVPM GGVFTTAKVR
EAFLSGPEAL PDLFHGYTYS GHPLASAAAI ATLDVYRDEG IFENAAKMAP IWEEMLHSFA
DVPDVIDIRN MGLIGAMEID PNSSRTAPEL AKKAWDIGLS FRPIGNNFAM SPPLTIDEEH
IGKVKDMLTK VLR
//
