ID Q98K53_RHILO Unreviewed; 442 AA.
AC Q98K53;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=Beta-alanine-pyruvate transaminase {ECO:0000313|EMBL:BAB48961.1};
GN OrderedLocusNames=mll1632 {ECO:0000313|EMBL:BAB48961.1};
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835 {ECO:0000313|EMBL:BAB48961.1, ECO:0000313|Proteomes:UP000000552};
RN [1] {ECO:0000313|EMBL:BAB48961.1, ECO:0000313|Proteomes:UP000000552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099
RC {ECO:0000313|Proteomes:UP000000552};
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR EMBL; BA000012; BAB48961.1; -; Genomic_DNA.
DR RefSeq; WP_010910314.1; NC_002678.2.
DR AlphaFoldDB; Q98K53; -.
DR GeneID; 66683276; -.
DR KEGG; mlo:mll1632; -.
DR PATRIC; fig|266835.9.peg.1316; -.
DR eggNOG; COG0161; Bacteria.
DR HOGENOM; CLU_016922_4_3_5; -.
DR Proteomes; UP000000552; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; 2.
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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Pyruvate {ECO:0000313|EMBL:BAB48961.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 442 AA; 48055 MW; 33EBC84A088255F1 CRC64;
MSNRLKVTPN DLSAFWMPFT ANRQFKQAPR MFVSAKDMHY TTSDGRKVLD GTAGLWCVNA
GHCRPKITEA IQHQAAELDY APAFQMGHPI VFELANRLVD IAPKGMDHVF FTNSGSESVE
TALKMAIAYH RMKGEGARTR LIGRERGYHG VNFGGISVGG IVSNRKMFGT LLGGVDHMPH
THLPEKNAFS KGVPEYGAEL ANELERIVAL HDASTIAAVI VEPVAGSTGV ILPPKGYLQK
LREICTKHGI LLIFDEVITG FGRLGAPFAA DYFGVVPDIM TTAKGVSNGV IPMGAVFVKK
EIHDAFMTGP EHMIEFFHGY TYSGNPIACA AALGTLDTYK EEGLLTRGEE LAPYWEDALH
SLKGEPHVID IRNIGLIGAI ELAPIAGSPT KRAFSAFVKA FERGALIRTT GDIIALSPPL
IITKGQINEL IDHVREVLRS ID
//
