AVTA_MYCTU
ID AVTA_MYCTU Reviewed; 388 AA.
AC P96847; F2GJR1; I6Y3W0;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Valine--pyruvate aminotransferase {ECO:0000305};
DE EC=2.6.1.66 {ECO:0000269|PubMed:32327655};
DE AltName: Full=Alanine--valine transaminase {ECO:0000305};
GN Name=aspB {ECO:0000303|PubMed:25005091};
GN OrderedLocusNames=Rv3565 {ECO:0000312|EMBL:CCP46387.1};
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].
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 [3]
RP CATALYTIC ACTIVITY.
RC STRAIN=H37Rv;
RX PubMed=32327655; DOI=10.1038/s41467-020-15876-8;
RA Jansen R.S., Mandyoli L., Hughes R., Wakabayashi S., Pinkham J.T.,
RA Selbach B., Guinn K.M., Rubin E.J., Sacchettini J.C., Rhee K.Y.;
RT "Aspartate aminotransferase Rv3722c governs aspartate-dependent nitrogen
RT metabolism in Mycobacterium tuberculosis.";
RL Nat. Commun. 11:1960-1960(2020).
RN [4]
RP CRYSTALLIZATION.
RX PubMed=25005091; DOI=10.1107/s2053230x14011820;
RA Saroj D.C., Singh K.H., Anant A., Biswal B.K.;
RT "Overexpression, purification, crystallization and structure determination
RT of AspB, a putative aspartate aminotransferase from Mycobacterium
RT tuberculosis.";
RL Acta Crystallogr. F Struct. Biol. Commun. 70:928-932(2014).
RN [5] {ECO:0007744|PDB:5YHV}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE
RP AND 2-OXOGLUTARIC ACID, AND COFACTOR.
RA Saroj D.C., Biswal B.K.;
RT "Crystal structure of an aminotransferase from Mycobacterium
RT tuberculosis.";
RL Submitted (SEP-2017) to the PDB data bank.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-valine + pyruvate = 3-methyl-2-oxobutanoate + L-alanine;
CC Xref=Rhea:RHEA:22912, ChEBI:CHEBI:11851, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:57762, ChEBI:CHEBI:57972; EC=2.6.1.66;
CC Evidence={ECO:0000269|PubMed:32327655};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|Ref.5};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46387.1; -; Genomic_DNA.
DR RefSeq; NP_218082.1; NC_000962.3.
DR RefSeq; WP_003419356.1; NZ_NVQJ01000014.1.
DR PDB; 5YHV; X-ray; 2.70 A; A/B/C/D=1-388.
DR PDBsum; 5YHV; -.
DR AlphaFoldDB; P96847; -.
DR SMR; P96847; -.
DR STRING; 83332.Rv3565; -.
DR PaxDb; P96847; -.
DR DNASU; 888305; -.
DR GeneID; 888305; -.
DR KEGG; mtu:Rv3565; -.
DR PATRIC; fig|83332.111.peg.3970; -.
DR TubercuList; Rv3565; -.
DR eggNOG; COG0436; Bacteria.
DR InParanoid; P96847; -.
DR OMA; IHMEVGQ; -.
DR PhylomeDB; P96847; -.
DR BRENDA; 2.6.1.1; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0009042; F:valine-pyruvate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.640.10; -; 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 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; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..388
FT /note="Valine--pyruvate aminotransferase"
FT /id="PRO_0000450668"
FT MOD_RES 234
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|Ref.5"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:5YHV"
FT HELIX 15..29
FT /evidence="ECO:0007829|PDB:5YHV"
FT HELIX 47..59
FT /evidence="ECO:0007829|PDB:5YHV"
FT HELIX 71..85
FT /evidence="ECO:0007829|PDB:5YHV"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:5YHV"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:5YHV"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:5YHV"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:5YHV"
FT HELIX 126..134
FT /evidence="ECO:0007829|PDB:5YHV"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:5YHV"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:5YHV"
FT HELIX 154..158
FT /evidence="ECO:0007829|PDB:5YHV"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:5YHV"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:5YHV"
FT HELIX 182..195
FT /evidence="ECO:0007829|PDB:5YHV"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:5YHV"
FT TURN 204..207
FT /evidence="ECO:0007829|PDB:5YHV"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:5YHV"
FT STRAND 224..236
FT /evidence="ECO:0007829|PDB:5YHV"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:5YHV"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:5YHV"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:5YHV"
FT HELIX 253..263
FT /evidence="ECO:0007829|PDB:5YHV"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:5YHV"
FT HELIX 269..275
FT /evidence="ECO:0007829|PDB:5YHV"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:5YHV"
FT HELIX 281..308
FT /evidence="ECO:0007829|PDB:5YHV"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:5YHV"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:5YHV"
FT HELIX 333..343
FT /evidence="ECO:0007829|PDB:5YHV"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:5YHV"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:5YHV"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:5YHV"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:5YHV"
FT HELIX 371..384
FT /evidence="ECO:0007829|PDB:5YHV"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:5YHV"
SQ SEQUENCE 388 AA; 41081 MW; C67411D91D79D329 CRC64;
MTDRVALRAG VPPFYVMDVW LAAAERQRTH GDLVNLSAGQ PSAGAPEPVR AAAAAALHLN
QLGYSVALGI PELRDAIAAD YQRRHGITVE PDAVVITTGS SGGFLLAFLA CFDAGDRVAM
ASPGYPCYRN ILSALGCEVV EIPCGPQTRF QPTAQMLAEI DPPLRGVVVA SPANPTGTVI
PPEELAAIAS WCDASDVRLI SDEVYHGLVY QGAPQTSCAW QTSRNAVVVN SFSKYYAMTG
WRLGWLLVPT VLRRAVDCLT GNFTICPPVL SQIAAVSAFT PEATAEADGN LASYAINRSL
LLDGLRRIGI DRLAPTDGAF YVYADVSDFT SDSLAFCSKL LADTGVAIAP GIDFDTARGG
SFVRISFAGP SGDIEEALRR IGSWLPSQ
