BIOF2_MYCTU
ID BIOF2_MYCTU Reviewed; 771 AA.
AC P9WQ85; L0T270; P71602; Q7DAK0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Putative 8-amino-7-oxononanoate synthase 2;
DE Short=AONS;
DE EC=2.3.1.47;
DE AltName: Full=7-keto-8-amino-pelargonic acid synthase;
DE Short=7-KAP synthase;
DE Short=KAPA synthase;
DE AltName: Full=8-amino-7-ketopelargonate synthase;
GN Name=bioF2; OrderedLocusNames=Rv0032;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SIMILARITY: In the C-terminal section; belongs to the class-II
CC pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP42754.1; -; Genomic_DNA.
DR PIR; F70701; F70701.
DR RefSeq; NP_214546.1; NC_000962.3.
DR RefSeq; WP_003905217.1; NZ_NVQJ01000005.1.
DR AlphaFoldDB; P9WQ85; -.
DR SMR; P9WQ85; -.
DR STRING; 83332.Rv0032; -.
DR PaxDb; P9WQ85; -.
DR DNASU; 887050; -.
DR GeneID; 887050; -.
DR KEGG; mtu:Rv0032; -.
DR TubercuList; Rv0032; -.
DR eggNOG; COG0156; Bacteria.
DR eggNOG; COG3146; Bacteria.
DR OMA; DALNHRG; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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 Pfam; PF13480; Acetyltransf_6; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..771
FT /note="Putative 8-amino-7-oxononanoate synthase 2"
FT /id="PRO_0000420959"
FT REGION 1..418
FT /note="Unknown"
FT REGION 419..771
FT /note="KAPA synthase"
FT BINDING 407
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 485..486
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 510
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 556
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 581..584
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 615
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
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
