ID C3MAN5_SINFN Unreviewed; 445 AA.
AC C3MAN5;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:ACP27028.1};
GN OrderedLocusNames=NGR_c32980 {ECO:0000313|EMBL:ACP27028.1};
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394 {ECO:0000313|EMBL:ACP27028.1, ECO:0000313|Proteomes:UP000001054};
RN [1] {ECO:0000313|EMBL:ACP27028.1, ECO:0000313|Proteomes:UP000001054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR EMBL; CP001389; ACP27028.1; -; Genomic_DNA.
DR RefSeq; WP_012709776.1; NC_012587.1.
DR RefSeq; YP_002827781.1; NC_012587.1.
DR AlphaFoldDB; C3MAN5; -.
DR STRING; 394.NGR_c32980; -.
DR KEGG; rhi:NGR_c32980; -.
DR PATRIC; fig|394.7.peg.6140; -.
DR eggNOG; COG0161; Bacteria.
DR HOGENOM; CLU_016922_4_0_5; -.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000001054; 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 ECO:0000313|EMBL:ACP27028.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 445 AA; 47971 MW; B2D58A0A8BD43108 CRC64;
MDAHNKPNTP ALDSYWMPFT ANRQFKAAPR LLASAEGMHY TSVDGRRILD GTAGLWCVNA
GHGRRQIAAA VERQLTTMDF APSFQMGHPI AFDFAERLAE IAPGPEGQKL DRVFFTGSGS
ESVDTALKIA LAYQRSIGQG TRTRLIGRER GYHGVGFGGI SVGGILNNRR VFPQLPGSDH
LRHTHDLARN AFVKGQPDHG AELADDLERL VALHGAETIA ACIVEPVAGS TGVLIPPKGY
LERLRAICNK HGILLIFDEV ITGFGRLGAA FAADYFNVTP DLVTTAKGLT NGAIPMGAVF
ASRKVHDALM HGPEGQIELF HGYTYSGHPA ACAAGIATLD IYRDEGLMTR AAELQDDWHE
AMHSLKGLPH VIDIRTIGLI AGIELQSRDG APGTRAYDVF VDCFEKGLLI RVTGDIIAFS
PPLIADKSHF GEIVSILGDA LKRVK
//
