ID A0A0M4MIM2_9SPHN Unreviewed; 608 AA.
AC A0A0M4MIM2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Probable branched-chain-amino-acid aminotransferase {ECO:0000256|ARBA:ARBA00014472};
GN ORFNames=AMC99_02343 {ECO:0000313|EMBL:ALE17618.1};
OS Altererythrobacter epoxidivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Altererythrobacter.
OX NCBI_TaxID=361183 {ECO:0000313|EMBL:ALE17618.1, ECO:0000313|Proteomes:UP000057938};
RN [1] {ECO:0000313|EMBL:ALE17618.1, ECO:0000313|Proteomes:UP000057938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7731 {ECO:0000313|EMBL:ALE17618.1,
RC ECO:0000313|Proteomes:UP000057938};
RA Li Z., Cheng H., Huo Y., Xu X.;
RT "Complete genome sequence of a benzo[a]pyrene-degrading bacterium
RT Altererythrobacter epoxidivorans CGMCC 1.7731T.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU004516};
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009320}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP012669; ALE17618.1; -; Genomic_DNA.
DR RefSeq; WP_061926662.1; NZ_CP012669.1.
DR AlphaFoldDB; A0A0M4MIM2; -.
DR STRING; 361183.AMC99_02343; -.
DR KEGG; aep:AMC99_02343; -.
DR PATRIC; fig|361183.4.peg.2301; -.
DR OrthoDB; 9803598at2; -.
DR Proteomes; UP000057938; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.470.10; -; 1.
DR Gene3D; 3.60.120.10; Anthranilate synthase; 1.
DR Gene3D; 3.20.10.10; D-amino Acid Aminotransferase, subunit A, domain 2; 1.
DR InterPro; IPR005802; ADC_synth_comp_1.
DR InterPro; IPR005801; ADC_synthase.
DR InterPro; IPR001544; Aminotrans_IV.
DR InterPro; IPR018300; Aminotrans_IV_CS.
DR InterPro; IPR036038; Aminotransferase-like.
DR InterPro; IPR019999; Anth_synth_I-like.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR InterPro; IPR015890; Chorismate_C.
DR NCBIfam; TIGR00553; pabB; 1.
DR PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR PANTHER; PTHR11236:SF18; AMINODEOXYCHORISMATE SYNTHASE; 1.
DR Pfam; PF01063; Aminotran_4; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR PRINTS; PR00095; ANTSNTHASEI.
DR SUPFAM; SSF56322; ADC synthase; 1.
DR SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:ALE17618.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004516};
KW Reference proteome {ECO:0000313|Proteomes:UP000057938}.
FT DOMAIN 133..389
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
SQ SEQUENCE 608 AA; 65225 MW; D136F3D24EF172E4 CRC64;
MGQNTPFILL DDARTDNPAP AHLYREPRQV FVARRGEEVS RVLAEADKAR LKTGGHLAGY
IAYEAGLALE PRLAGRVDGR SGAAGPLVWL GLFDDAEEIA PDDVAAWLAS QAAEDDGGDA
ALGPLVPQLS TGGYEAAFAT MQEAIRAGDI YQTNLTYPLA GSYRGSPVAI YAALRPAAKA
GYGGLIFDGS NWLLSLSPEL FVSLRGDAAK VKPMKGTRPR AADESADEAL RDELAMSEKD
KAENLMIVDL MRNDLSRVAE PGSVTVEGLF SVETYPTVHQ MVSTVHARLE DGKGAVDLVR
AIFPCGSITG APKIRAMELI DEVERDPRGP YCGAIGRIDP DGSAAFNVAI RTLRLTPIEN
SQGAAVMGVG SAIVADSEPL AERRECEIKG GFARSSTSDH RAARFDLIES MLFDPEAGIS
LLELHLERIK QSAAELGFSF DRHDVRNQIQ ALCFDLEHRS KVRLLAARSG AIAFEATRIE
QVAKPVLQCI ALPLPVDPGD WRLRHKTSER AFYEEALGVA RGMGADEALL VRDDGLVTEG
SFTNIFVRGD DGILLTPPTA LGLLPGVLRR SLIDAGKARE AELSLEDLEG GFLLGNSVRG
LVEAEFTS
//
