ID B8IGY8_METNO Unreviewed; 457 AA.
AC B8IGY8;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:ACL57863.1};
GN OrderedLocusNames=Mnod_2912 {ECO:0000313|EMBL:ACL57863.1};
OS Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL57863.1, ECO:0000313|Proteomes:UP000008207};
RN [1] {ECO:0000313|EMBL:ACL57863.1, ECO:0000313|Proteomes:UP000008207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC {ECO:0000313|Proteomes:UP000008207};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Marx C.J.,
RA Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium nodulans ORS 2060.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001349; ACL57863.1; -; Genomic_DNA.
DR RefSeq; WP_015929538.1; NC_011894.1.
DR AlphaFoldDB; B8IGY8; -.
DR STRING; 460265.Mnod_2912; -.
DR KEGG; mno:Mnod_2912; -.
DR eggNOG; COG0161; Bacteria.
DR HOGENOM; CLU_016922_4_1_5; -.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000008207; 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 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:0000313|EMBL:ACL57863.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000008207};
KW Transferase {ECO:0000313|EMBL:ACL57863.1}.
SQ SEQUENCE 457 AA; 48832 MW; F790D6280CDDEED8 CRC64;
MFSNSLIELD RAHLVHPVAS YRGHERTGVR VLRSAKGATV TDAAGRELLD GFAGLWCVNA
GYGHDSIVEA AARQMRELPY ATAYFGLGSE PAIRLAAALA ERAPGDLNHV YFTLGGSDAV
DTTVRLIRNY QTVRGKPEKD QFISLEQGYH GSSTVGAGLT ALPAFHANFG LPFAWQHKIP
SPYPYRNPAG SDLEAIIAAS LAALRAKVEE LGPERVAAFY AEPIQGSGGV IVPPRGWMKA
MRDLCAELDI LFVADEVITG FGRTGPLFAC TEDEVVPDLM TTAKGLTSGY VPMGAVFLSN
RIYDTIADGA GEAAIGHGYT YSAHPVSAAV GLEVLRLYEN GLLENGRRAG TRLQAGLQSL
ADHPLVGDVR GRGLLAALEL VVDKARKAPL PAAADPARRI FDRAWNNGLV IRAFGNGILG
YAPPLCCTEA EIDAIVERTR RILDQTLEDA DVRAAMA
//
