ID A5TYA3_MYCTA Unreviewed; 771 AA.
AC A5TYA3;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=8-amino-7-oxononanoate synthase {ECO:0000256|ARBA:ARBA00013187};
DE EC=2.3.1.47 {ECO:0000256|ARBA:ARBA00013187};
DE AltName: Full=7-keto-8-amino-pelargonic acid synthase {ECO:0000256|ARBA:ARBA00032610};
DE AltName: Full=8-amino-7-ketopelargonate synthase {ECO:0000256|ARBA:ARBA00033381};
GN Name=bioF2 {ECO:0000313|EMBL:ABQ71753.1};
GN OrderedLocusNames=MRA_0035 {ECO:0000313|EMBL:ABQ71753.1};
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=419947 {ECO:0000313|EMBL:ABQ71753.1, ECO:0000313|Proteomes:UP000001988};
RN [1] {ECO:0000313|EMBL:ABQ71753.1, ECO:0000313|Proteomes:UP000001988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25177 / H37Ra {ECO:0000313|Proteomes:UP000001988};
RX PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA Wang H., Wang S., Zhao G., Zhang Y.;
RT "Genetic basis of virulence attenuation revealed by comparative genomic
RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL PLoS ONE 3:E2375-E2375(2008).
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; CP000611; ABQ71753.1; -; Genomic_DNA.
DR RefSeq; WP_003905217.1; NZ_CP016972.1.
DR AlphaFoldDB; A5TYA3; -.
DR SMR; A5TYA3; -.
DR KEGG; mra:MRA_0035; -.
DR eggNOG; COG0156; Bacteria.
DR eggNOG; COG3146; Bacteria.
DR HOGENOM; CLU_024741_1_0_11; -.
DR Proteomes; UP000001988; Chromosome.
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 Gene3D; 3.40.630.30; -; 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; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR038740; BioF2-like_GNAT_dom.
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; PF13480; Acetyltransf_6; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 4: Predicted;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000001988}.
FT DOMAIN 190..307
FT /note="BioF2-like acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13480"
FT DOMAIN 418..756
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 771 AA; 86243 MW; 8FC1D0FED27E43C6 CRC64;
MPTGLGYDFL RPVEDSGIND LKHYYFMADL ADGQPLGRAN LYSVCFDLAT TDRKLTPAWR
TTIKRWFPGF MTFRFLECGL LTMVSNPLAL RSDTDLERVL PVLAGQMDQL AHDDGSDFLM
IRDVDPEHYQ RYLDILRPLG FRPALGFSRV DTTISWSSVE EALGCLSHKR RLPLKTSLEF
RERFGIEVEE LDEYAEHAPV LARLWRNVKT EAKDYQREDL NPEFFAACSR HLHGRSRLWL
FRYQGTPIAF FLNVWGADEN YILLEWGIDR DFEHYRKANL YRAALMLSLK DAISRDKRRM
EMGITNYFTK LRIPGARVIP TIYFLRHSTD PVHTATLARM MMHNIQRPTL PDDMSEEFCR
WEERIRLDQD GLPEHDIFRK IDRQHKYTGL KLGGVYGFYP RFTGPQRSTV KAAELGEIVL
LGTNSYLGLA THPEVVEASA EATRRYGTGC SGSPLLNGTL DLHVSLEQEL ACFLGKPAAV
LCSTGYQSNL AAISALCESG DMIIQDALNH RSLFDAARLS GADFTLYRHN DMDHLARVLR
RTEGRRRIIV VDAVFSMEGT VADLATIAEL ADRHGCRVYV DESHALGVLG PDGRGASAAL
GVLARMDVVM GTFSKSFASV GGFIAGDRPV VDYIRHNGSG HVFSASLPPA AAAATHAALR
VSRREPDRRA RVLAAAEYMA TGLARQGYQA EYHGTAIVPV ILGNPTVAHA GYLRLMRSGV
YVNPVAPPAV PEERSGFRTS YLADHRQSDL DRALHVFAGL AEDLTPQGAA L
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