ID A0A1M6MUT6_9CLOT Unreviewed; 396 AA.
AC A0A1M6MUT6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=8-amino-7-ketopelargonate synthase {ECO:0000256|RuleBase:RU003693};
DE EC=2.3.1.47 {ECO:0000256|RuleBase:RU003693};
GN ORFNames=SAMN02745883_00652 {ECO:0000313|EMBL:SHJ87231.1};
OS Caminicella sporogenes DSM 14501.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Caminicella.
OX NCBI_TaxID=1121266 {ECO:0000313|EMBL:SHJ87231.1, ECO:0000313|Proteomes:UP000184082};
RN [1] {ECO:0000313|EMBL:SHJ87231.1, ECO:0000313|Proteomes:UP000184082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14501 {ECO:0000313|EMBL:SHJ87231.1,
RC ECO:0000313|Proteomes:UP000184082};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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, ECO:0000256|RuleBase:RU003693}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-
CC oxononanoate + CO2 + holo-[ACP]; Xref=Rhea:RHEA:42288, Rhea:RHEA-
CC COMP:9685, Rhea:RHEA-COMP:9955, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57972, ChEBI:CHEBI:64479, ChEBI:CHEBI:78846,
CC ChEBI:CHEBI:149468; EC=2.3.1.47;
CC Evidence={ECO:0000256|ARBA:ARBA00034067,
CC ECO:0000256|RuleBase:RU003693};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR604723-51, ECO:0000256|RuleBase:RU003693};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004746, ECO:0000256|RuleBase:RU003693}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU003693}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. BioF subfamily.
CC {ECO:0000256|ARBA:ARBA00010008, ECO:0000256|RuleBase:RU003693}.
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DR EMBL; FRAJ01000005; SHJ87231.1; -; Genomic_DNA.
DR RefSeq; WP_072965950.1; NZ_FRAJ01000005.1.
DR AlphaFoldDB; A0A1M6MUT6; -.
DR STRING; 1121266.SAMN02745883_00652; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000184082; Unassembled WGS sequence.
DR GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR010962; AONS_Archaea/Firmicutes.
DR InterPro; IPR004723; AONS_Archaea/Proteobacteria.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00858; bioF; 1.
DR NCBIfam; TIGR01825; gly_Cac_T_rel; 1.
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 Biotin biosynthesis {ECO:0000256|ARBA:ARBA00022756};
KW Ligase {ECO:0000313|EMBL:SHJ87231.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604723-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000184082};
KW Transferase {ECO:0000256|RuleBase:RU003693}.
FT DOMAIN 42..384
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT MOD_RES 243
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604723-51"
SQ SEQUENCE 396 AA; 43669 MW; 91DB69325A18E0B9 CRC64;
MSNVHELKFL KEKIEELKKQ GVYRKLPVLE GANEAEVILN GKKVINLSSN NYLGFANHPR
LKKAAIEAVE KYGVGAGAVR TIVGNMDIHE EMEKVLAEFK REEAVMVFQS GFNCNAGTIQ
AITEKGDLIV SDELNHASII DGARLSKADK TIYKHNDMDD LERVLKENRD KYRNILIITD
GVFSMDGDIA NLPDIVELAE KYEAMTYVDD AHGSGVLGEN GRGTVDHFGL HGRIDFSIGT
LSKAIGVIGG YVAGSKTMQD WLSHRGRPLL FSTSLPPAAV GAIIEAVKML MESSEYTDRL
WANAKFFKER LGKLGFNTGN SQTPITPVII GDEAKTMEFS RKLFENGVFV SGIVYPTVPK
GTGRVRCMVT AGHTTEQLER AVEVFEKVGK EMKILK
//
