ID U2ELQ0_9FIRM Unreviewed; 395 AA.
AC U2ELQ0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Putative 8-amino-7-oxononanoate synthase {ECO:0000313|EMBL:ERI95632.1};
GN ORFNames=HMPREF1982_00106 {ECO:0000313|EMBL:ERI95632.1};
OS Clostridiales bacterium oral taxon 876 str. F0540.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=1321778 {ECO:0000313|EMBL:ERI95632.1, ECO:0000313|Proteomes:UP000016490};
RN [1] {ECO:0000313|EMBL:ERI95632.1, ECO:0000313|Proteomes:UP000016490}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0540 {ECO:0000313|EMBL:ERI95632.1,
RC ECO:0000313|Proteomes:UP000016490};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-
CC carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON),
CC [acyl-carrier protein], and carbon dioxide.
CC {ECO:0000256|ARBA:ARBA00002513}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU003693};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003693}.
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:ERI95632.1}.
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; AWSZ01000003; ERI95632.1; -; Genomic_DNA.
DR AlphaFoldDB; U2ELQ0; -.
DR STRING; 1321778.HMPREF1982_00106; -.
DR PATRIC; fig|1321778.3.peg.108; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_0_9; -.
DR OrthoDB; 9807157at2; -.
DR Proteomes; UP000016490; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd06454; KBL_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; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR PANTHER; PTHR13693:SF3; LD36009P; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003693};
KW Reference proteome {ECO:0000313|Proteomes:UP000016490}.
FT DOMAIN 43..383
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 395 AA; 43370 MW; 19FB2A99260FDCC4 CRC64;
MVDIFEKCYN FTEAKEAIKA GIYPYFHALT SGQDTEVIMN GKRVIMLGSN NYLGLTSDPR
LKKAAIEAVE KYGSGCSGSR FLNGTLDLHI ELEKKLAAFV RKEAALVFST GFQTNLGILS
AIAGKNDYII GDRQNHASIV DACRLSFAKL LKFKHNDMQD LKRVLEYIPE DSGKIIVVDG
VFSMEGDIAN LPEIVKLAKQ YGARVMVDDA HGLGVMGEHG RGTAEYFGLE DEVDIVMGTF
SKSLASLGGY VAAKEEVIHY IKHHSRPFIF SASIPPANAA AAMEALNILE QEPERVKRLW
ENAEFMKAGF KAMGLSVGET QTPIVPIVVG DDYRAFALTM ELLNEGVYVN PAVSPAVEKG
CALLRTSYTP THTREQLEFA LKAFERVLGN KEQTA
//
