BACF_BACSU
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 03-AUG-2022, entry version 135.
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}; OrderedLocusNames=BSU37690;
GN ORFNames=ipa-85d;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; 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; NZ_JNCM01000034.1.
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 PDBsum; 6L1L; -.
DR PDBsum; 6L1N; -.
DR PDBsum; 6L1O; -.
DR AlphaFoldDB; P39643; -.
DR SMR; P39643; -.
DR STRING; 224308.BSU37690; -.
DR PaxDb; P39643; -.
DR PRIDE; P39643; -.
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 OMA; FYLYVEI; -.
DR PhylomeDB; P39643; -.
DR BioCyc; BSUB:BSU37690-MON; -.
DR BioCyc; MetaCyc:MON-19128; -.
DR UniPathway; UPA00100; -.
DR Proteomes; UP000001570; Chromosome.
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 Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
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 Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
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 17..28
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 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 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"
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
