ID   BACF_BACSU              Reviewed;         399 AA.
AC   P39643;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   02-SEP-2026, entry version 149.
DE   RecName: Full=Transaminase BacF {ECO:0000303|PubMed:20052993};
DE            EC=2.6.1.- {ECO:0000269|PubMed:20052993, ECO:0000269|PubMed:22765234};
DE   AltName: Full=Transaminase A;
GN   Name=bacF {ECO:0000303|PubMed:22765234};
GN   Synonyms=ywfG {ECO:0000303|PubMed:20052993};
GN   OrderedLocusNames=BSU37690; ORFNames=ipa-85d;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA   Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA   Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA   Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT   "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT   region from 325 degrees to 333 degrees.";
RL   Mol. Microbiol. 10:371-384(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   INDUCTION, AND PATHWAY.
RC   STRAIN=168 / 61884;
RX   PubMed=12372825; DOI=10.1074/jbc.m208722200;
RA   Inaoka T., Takahashi K., Ohnishi-Kameyama M., Yoshida M., Ochi K.;
RT   "Guanine nucleotides guanosine 5'-diphosphate 3'-diphosphate and GTP co-
RT   operatively regulate the production of an antibiotic bacilysin in Bacillus
RT   subtilis.";
RL   J. Biol. Chem. 278:2169-2176(2003).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=20052993; DOI=10.1021/bi9021186;
RA   Mahlstedt S.A., Walsh C.T.;
RT   "Investigation of anticapsin biosynthesis reveals a four-enzyme pathway to
RT   tetrahydrotyrosine in Bacillus subtilis.";
RL   Biochemistry 49:912-923(2010).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBSTRATE SPECIFICITY.
RX   PubMed=22765234; DOI=10.1021/bi3006362;
RA   Parker J.B., Walsh C.T.;
RT   "Stereochemical outcome at four stereogenic centers during conversion of
RT   prephenate to tetrahydrotyrosine by BacABGF in the bacilysin pathway.";
RL   Biochemistry 51:5622-5632(2012).
CC   -!- FUNCTION: Part of the bacABCDEF operon responsible for the biosynthesis
CC       of the nonribosomally synthesized dipeptide antibiotic bacilysin,
CC       composed of L-alanine and L-anticapsin. Bacilysin is an irreversible
CC       inactivator of the glutaminase domain of glucosamine synthetase
CC       (PubMed:20052993). Catalyzes the reductive amination of the C2 ketone
CC       of tetrahydro-hydroxyphenylpyruvate (H4HPP), with L-Phe as an amino
CC       donor, to yield tetrahydrotyrosine (H4Tyr) diastereomer
CC       (PubMed:22765234). D-Phe is not an effective amino donor
CC       (PubMed:22765234). BacF associated to BacG converts 3E,7R- and 3Z,7R-
CC       ex-H2HPP to 2S,4R,7R- and 2S,4S,7R-H4Tyr, respectively. Given that
CC       bacilysin has the 2S,4S stereochemistry in its anticapsin moiety, it is
CC       likely that the 2S,4S-H4Tyr is the diastereomer used for the
CC       biosynthesis (PubMed:22765234). {ECO:0000269|PubMed:20052993,
CC       ECO:0000269|PubMed:22765234}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:Q93ZN9};
CC   -!- PATHWAY: Antibiotic biosynthesis; bacilysin biosynthesis.
CC       {ECO:0000305|PubMed:12372825, ECO:0000305|PubMed:20052993,
CC       ECO:0000305|PubMed:22765234}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q93ZN9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: The compound guanosine 5'-diphosphate 3'-diphosphate (ppGpp)
CC       is essential for the transcription of the bacABCDEF operon and BacG,
CC       and GTP regulates the transcription of both this operon and ywfH via
CC       the CodY-mediated regulation system. {ECO:0000269|PubMed:12372825}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; X73124; CAA51641.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15796.1; -; Genomic_DNA.
DR   PIR; S39740; S39740.
DR   RefSeq; NP_391649.1; NC_000964.3.
DR   RefSeq; WP_003242568.1; NC_000964.3.
DR   PDB; 6L1L; X-ray; 1.90 A; A/B=1-399.
DR   PDB; 6L1N; X-ray; 2.00 A; A/B=1-399.
DR   PDB; 6L1O; X-ray; 1.90 A; A/B=1-399.
DR   AlphaFoldDB; P39643; -.
DR   SMR; P39643; -.
DR   FunCoup; P39643; 79.
DR   STRING; 224308.BSU37690; -.
DR   PaxDb; 224308-BSU37690; -.
DR   EnsemblBacteria; CAB15796; CAB15796; BSU_37690.
DR   GeneID; 937157; -.
DR   KEGG; bsu:BSU37690; -.
DR   PATRIC; fig|224308.179.peg.4081; -.
DR   eggNOG; COG0436; Bacteria.
DR   InParanoid; P39643; -.
DR   OrthoDB; 9802328at2; -.
DR   PhylomeDB; P39643; -.
DR   BioCyc; BSUB:BSU37690-MONOMER; -.
DR   BioCyc; MetaCyc:MONOMER-19128; -.
DR   UniPathway; UPA00100; -.
DR   Proteomes; UP000001570; Chromosome.
DR   AbasyAtlas; P39643; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IDA:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR   CDD; cd00609; AAT_like; 1.
DR   FunFam; 3.40.640.10:FF:000218; Aminotransferase; 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; IPR004839; Aminotransferase_I/II_large.
DR   InterPro; IPR050881; LL-DAP_aminotransferase.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; NF005977; PRK08068.1; 1.
DR   PANTHER; PTHR42832; AMINO ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42832:SF3; L-GLUTAMINE--4-(METHYLSULFANYL)-2-OXOBUTANOATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
DR   PDBsum; 6L1L; -.
DR   PDBsum; 6L1N; -.
DR   PDBsum; 6L1O; -.
PE   1: Evidence at protein level;
KW   3D-structure; Aminotransferase; Antibiotic biosynthesis; Cytoplasm;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..399
FT                   /note="Transaminase BacF"
FT                   /id="PRO_0000123837"
FT   BINDING         103..104
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT   BINDING         128
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT   BINDING         178
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT   BINDING         209
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT   BINDING         236..238
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT   BINDING         247
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT   MOD_RES         239
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q93ZN9"
FT   HELIX           6..10
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   HELIX           12..14
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   HELIX           17..28
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   HELIX           45..47
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   HELIX           48..57
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   HELIX           61..63
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   HELIX           73..87
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   TURN            93..95
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   STRAND          96..102
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   HELIX           103..114
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   STRAND          120..126
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   HELIX           130..137
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   STRAND          141..146
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   HELIX           149..151
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   HELIX           157..159
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   TURN            162..167
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   STRAND          168..173
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   TURN            178..180
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   HELIX           186..198
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   STRAND          202..206
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   TURN            208..211
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   STRAND          213..216
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   HELIX           217..220
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   HELIX           221..223
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   HELIX           227..230
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   STRAND          231..237
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   TURN            238..242
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   HELIX           244..246
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   STRAND          249..253
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   HELIX           255..268
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   HELIX           274..285
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   HELIX           289..313
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   HELIX           318..320
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   STRAND          321..329
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   HELIX           337..347
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   HELIX           355..358
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   HELIX           360..362
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   STRAND          365..369
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   HELIX           374..385
FT                   /evidence="ECO:0007829|PDB:6L1L"
FT   TURN            386..388
FT                   /evidence="ECO:0007829|PDB:6L1L"
SQ   SEQUENCE   399 AA;  44703 MW;  ED2026904513DDF3 CRC64;
     MEITPSDVIK TLPRQEFSLV FQKVKEMEKT GAHIINLGQG NPDLPTPPHI VEALREASLN
     PSFHGYGPFR GYPFLKEAIA AFYKREYGVT INPETEVALF GGGKAGLYVL TQCLLNPGDI
     ALVPNPGYPE YLSGITMARA ELYEMPLYEE NGYLPDFEKI DPAVLEKAKL MFLNYPNNPT
     GAVADAAFYA KAAAFAKEHN IHLIHDFAYG AFEFDQKPAS FLEAEDAKTV GAELYSFSKT
     FNMAGWRMAF AVGNEKIIQA VNEFQDHVFV GMFGGLQQAA SAALSGDPEH TESLKRIYKE
     RIDFFTALCE KELGWKMEKP KGTFYVWAEI PNTFETSHQF SDYLLEHAHV VVTPGEIFGS
     NGKRHVRISM VSKQEDLREF VTRIQKLNLP FGSLQETSR
//