BIOA_MYCTU
ID BIOA_MYCTU Reviewed; 437 AA.
AC P9WQ81; L0T781; O06622; P0A4X6;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000255|HAMAP-Rule:MF_00834};
DE EC=2.6.1.62 {ECO:0000269|PubMed:16984394, ECO:0000269|PubMed:20565114};
DE AltName: Full=7,8-diamino-pelargonic acid aminotransferase {ECO:0000255|HAMAP-Rule:MF_00834};
DE Short=DAPA AT {ECO:0000255|HAMAP-Rule:MF_00834};
DE Short=DAPA aminotransferase {ECO:0000255|HAMAP-Rule:MF_00834};
DE AltName: Full=7,8-diaminononanoate synthase {ECO:0000255|HAMAP-Rule:MF_00834};
DE Short=DANS {ECO:0000255|HAMAP-Rule:MF_00834};
DE AltName: Full=7,8-diaminopelargonic acid synthase {ECO:0000303|PubMed:20565114};
DE Short=DAPAS {ECO:0000303|PubMed:20565114};
DE AltName: Full=Diaminopelargonic acid synthase;
GN Name=bioA; OrderedLocusNames=Rv1568; ORFNames=MTCY336.35c;
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 DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=14569030; DOI=10.1073/pnas.2134250100;
RA Sassetti C.M., Rubin E.J.;
RT "Genetic requirements for mycobacterial survival during infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12989-12994(2003).
RN [3]
RP FUNCTION AS A ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE,
RP CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVITY REGULATION, REACTION
RP MECHANISM, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16984394; DOI=10.1111/j.1742-4658.2006.05479.x;
RA Mann S., Ploux O.;
RT "7,8-Diaminoperlargonic acid aminotransferase from Mycobacterium
RT tuberculosis, a potential therapeutic target. Characterization and
RT inhibition studies.";
RL FEBS J. 273:4778-4789(2006).
RN [4]
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).
RN [5] {ECO:0007744|PDB:3BV0, ECO:0007744|PDB:3LV2}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE
RP AND SUBSTRATE, MUTAGENESIS OF TYR-25, FUNCTION, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM,
RP AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20565114; DOI=10.1021/bi902097j;
RA Dey S., Lane J.M., Lee R.E., Rubin E.J., Sacchettini J.C.;
RT "Structural characterization of the Mycobacterium tuberculosis biotin
RT biosynthesis enzymes 7,8-diaminopelargonic acid synthase and dethiobiotin
RT synthetase.";
RL Biochemistry 49:6746-6760(2010).
CC -!- FUNCTION: Catalyzes the reversible transfer of the alpha-amino group
CC from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid
CC (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only
CC aminotransferase known to utilize SAM as an amino donor
CC (PubMed:20565114, PubMed:16984394). Can also use sinefungin but not S-
CC adenosylhomocysteine as substrate (PubMed:20565114).
CC {ECO:0000269|PubMed:16984394, ECO:0000269|PubMed:20565114}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine =
CC (7R,8S)-7,8-diammoniononanoate + S-adenosyl-4-methylsulfanyl-2-
CC oxobutanoate; Xref=Rhea:RHEA:16861, ChEBI:CHEBI:16490,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:149468, ChEBI:CHEBI:149469;
CC EC=2.6.1.62; Evidence={ECO:0000255|HAMAP-Rule:MF_00834,
CC ECO:0000269|PubMed:16984394, ECO:0000269|PubMed:20565114};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00834,
CC ECO:0000269|PubMed:16984394, ECO:0000269|PubMed:20565114};
CC -!- ACTIVITY REGULATION: Competitively inhibited by KAPA at concentrations
CC above 10 uM and by amiclenomycin. {ECO:0000269|PubMed:16984394}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.8 uM for KAPA (at pH 8.6 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:16984394};
CC KM=450 uM for SAM (at pH 8.5 at room temperature)
CC {ECO:0000269|PubMed:20565114};
CC KM=700 uM for sinefungin (at pH 8.5 at room temperature)
CC {ECO:0000269|PubMed:20565114};
CC Vmax=22 umol/min/mg enzyme (at pH 8.6 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:16984394};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
CC diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00834}.
CC -!- SUBUNIT: Homotetramer (PubMed:16984394). Homodimer (PubMed:20565114).
CC {ECO:0000269|PubMed:16984394, ECO:0000269|PubMed:20565114}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00834}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are shown to be highly
CC attenuated in a mouse tuberculosis model.
CC {ECO:0000269|PubMed:14569030}.
CC -!- MISCELLANEOUS: Catalysis proceeds by a classical ping-pong bi-bi
CC reaction mechanism. {ECO:0000269|PubMed:16984394}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. BioA subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00834, ECO:0000305}.
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DR EMBL; AL123456; CCP44332.1; -; Genomic_DNA.
DR PIR; B70540; B70540.
DR RefSeq; NP_216084.1; NC_000962.3.
DR RefSeq; WP_003407803.1; NZ_NVQJ01000004.1.
DR PDB; 3BV0; X-ray; 2.21 A; A/B=1-437.
DR PDB; 3LV2; X-ray; 2.18 A; A/B=1-437.
DR PDB; 3TFT; X-ray; 1.95 A; A/B=1-437.
DR PDB; 3TFU; X-ray; 1.94 A; A/B=1-437.
DR PDB; 4CXQ; X-ray; 1.80 A; A/B=1-437.
DR PDB; 4CXR; X-ray; 1.70 A; A/B=1-437.
DR PDB; 4MQP; X-ray; 1.83 A; A/B=1-437.
DR PDB; 4MQQ; X-ray; 1.70 A; A/B=1-437.
DR PDB; 4MQR; X-ray; 2.10 A; A/B=1-437.
DR PDB; 4W1V; X-ray; 2.24 A; A/B=7-435.
DR PDB; 4W1W; X-ray; 1.90 A; A/B=8-436.
DR PDB; 4W1X; X-ray; 1.80 A; A/B=1-437.
DR PDB; 4WYA; X-ray; 2.50 A; A/B/C/D=1-437.
DR PDB; 4WYC; X-ray; 1.70 A; A/B=7-437.
DR PDB; 4WYD; X-ray; 1.35 A; A/B=1-437.
DR PDB; 4WYE; X-ray; 1.75 A; A/B=1-437.
DR PDB; 4WYF; X-ray; 2.25 A; A/B=1-437.
DR PDB; 4WYG; X-ray; 1.62 A; A/B=1-437.
DR PDB; 4XEW; X-ray; 2.47 A; A/B=1-437.
DR PDB; 4XJL; X-ray; 1.85 A; A/B=1-437.
DR PDB; 4XJM; X-ray; 1.60 A; A/B=1-437.
DR PDB; 4XJO; X-ray; 1.50 A; A/B=1-437.
DR PDB; 4XJP; X-ray; 1.60 A; A/B=1-437.
DR PDBsum; 3BV0; -.
DR PDBsum; 3LV2; -.
DR PDBsum; 3TFT; -.
DR PDBsum; 3TFU; -.
DR PDBsum; 4CXQ; -.
DR PDBsum; 4CXR; -.
DR PDBsum; 4MQP; -.
DR PDBsum; 4MQQ; -.
DR PDBsum; 4MQR; -.
DR PDBsum; 4W1V; -.
DR PDBsum; 4W1W; -.
DR PDBsum; 4W1X; -.
DR PDBsum; 4WYA; -.
DR PDBsum; 4WYC; -.
DR PDBsum; 4WYD; -.
DR PDBsum; 4WYE; -.
DR PDBsum; 4WYF; -.
DR PDBsum; 4WYG; -.
DR PDBsum; 4XEW; -.
DR PDBsum; 4XJL; -.
DR PDBsum; 4XJM; -.
DR PDBsum; 4XJO; -.
DR PDBsum; 4XJP; -.
DR AlphaFoldDB; P9WQ81; -.
DR SMR; P9WQ81; -.
DR STRING; 83332.Rv1568; -.
DR ChEMBL; CHEMBL2146299; -.
DR PaxDb; P9WQ81; -.
DR DNASU; 886343; -.
DR GeneID; 45425552; -.
DR GeneID; 886343; -.
DR KEGG; mtu:Rv1568; -.
DR TubercuList; Rv1568; -.
DR eggNOG; COG0161; Bacteria.
DR OMA; VAVKMCL; -.
DR PhylomeDB; P9WQ81; -.
DR BRENDA; 2.6.1.62; 3445.
DR UniPathway; UPA00078; UER00160.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IDA:MTBBASE.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009102; P:biotin biosynthetic process; IDA:MTBBASE.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00834; BioA; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR005815; BioA.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00508; bioA; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Biotin biosynthesis; Cytoplasm;
KW Pyridoxal phosphate; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..437
FT /note="Adenosylmethionine-8-amino-7-oxononanoate
FT aminotransferase"
FT /id="PRO_0000120374"
FT BINDING 64
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_note="substrate"
FT /evidence="ECO:0000269|PubMed:20565114"
FT BINDING 124..125
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 157
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_note="substrate"
FT /evidence="ECO:0000269|PubMed:20565114"
FT BINDING 254
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 316
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_note="substrate"
FT /evidence="ECO:0000269|PubMed:20565114"
FT BINDING 317..318
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 400
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_note="substrate"
FT /evidence="ECO:0000305|PubMed:20565114"
FT SITE 25
FT /note="Participates in the substrate recognition with KAPA
FT and in a stacking interaction with the adenine ring of SAM"
FT /evidence="ECO:0000305|PubMed:20565114"
FT MOD_RES 283
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:20565114,
FT ECO:0007744|PDB:3BV0, ECO:0007744|PDB:3LV2"
FT MUTAGEN 25
FT /note="Y->A: Does not show detectable activity at 335 nm
FT with SAM, even up to concentrations of 3 mM, and shows
FT approximately 70% reduced activity with high concentrations
FT of DAPA (0.5 mM)."
FT /evidence="ECO:0000269|PubMed:20565114"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:4WYD"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:4WYD"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:4WYD"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:4WYD"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:4WYD"
FT HELIX 74..86
FT /evidence="ECO:0007829|PDB:4WYD"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:4WYD"
FT HELIX 98..110
FT /evidence="ECO:0007829|PDB:4WYD"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:4WYD"
FT HELIX 124..141
FT /evidence="ECO:0007829|PDB:4WYD"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:4WYD"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:4WYD"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:4WYD"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:4WYF"
FT HELIX 176..181
FT /evidence="ECO:0007829|PDB:4WYD"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:4WYD"
FT HELIX 197..210
FT /evidence="ECO:0007829|PDB:4WYD"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:4WYD"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:4WYD"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:4WYD"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:4WYD"
FT HELIX 235..247
FT /evidence="ECO:0007829|PDB:4WYD"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:4WYD"
FT TURN 256..263
FT /evidence="ECO:0007829|PDB:4WYD"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:4WYD"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:4WYD"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:4WYD"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:4WYD"
FT STRAND 293..298
FT /evidence="ECO:0007829|PDB:4WYD"
FT HELIX 299..305
FT /evidence="ECO:0007829|PDB:4WYD"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:4XJM"
FT TURN 318..321
FT /evidence="ECO:0007829|PDB:4WYD"
FT HELIX 323..337
FT /evidence="ECO:0007829|PDB:4WYD"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:4XJO"
FT HELIX 341..356
FT /evidence="ECO:0007829|PDB:4WYD"
FT HELIX 357..361
FT /evidence="ECO:0007829|PDB:4WYD"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:4WYD"
FT STRAND 375..381
FT /evidence="ECO:0007829|PDB:4WYD"
FT HELIX 385..393
FT /evidence="ECO:0007829|PDB:4WYD"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:4WYD"
FT STRAND 405..408
FT /evidence="ECO:0007829|PDB:4WYD"
FT HELIX 416..433
FT /evidence="ECO:0007829|PDB:4WYD"
SQ SEQUENCE 437 AA; 46319 MW; 8E6B6EDE4F0AE7F6 CRC64;
MAAATGGLTP EQIIAVDGAH LWHPYSSIGR EAVSPVVAVA AHGAWLTLIR DGQPIEVLDA
MSSWWTAIHG HGHPALDQAL TTQLRVMNHV MFGGLTHEPA ARLAKLLVDI TPAGLDTVFF
SDSGSVSVEV AAKMALQYWR GRGLPGKRRL MTWRGGYHGD TFLAMSICDP HGGMHSLWTD
VLAAQVFAPQ VPRDYDPAYS AAFEAQLAQH AGELAAVVVE PVVQGAGGMR FHDPRYLHDL
RDICRRYEVL LIFDEIATGF GRTGALFAAD HAGVSPDIMC VGKALTGGYL SLAATLCTAD
VAHTISAGAA GALMHGPTFM ANPLACAVSV ASVELLLGQD WRTRITELAA GLTAGLDTAR
ALPAVTDVRV CGAIGVIECD RPVDLAVATP AALDRGVWLR PFRNLVYAMP PYICTPAEIT
QITSAMVEVA RLVGSLP
