Y3778_MYCTU
ID Y3778_MYCTU Reviewed; 398 AA.
AC P9WQ67; L0TF82; P72044; Q7D4V8;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Uncharacterized protein Rv3778c;
GN OrderedLocusNames=Rv3778c;
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=12657046; DOI=10.1046/j.1365-2958.2003.03425.x;
RA Sassetti C.M., Boyd D.H., Rubin E.J.;
RT "Genes required for mycobacterial growth defined by high density
RT mutagenesis.";
RL Mol. Microbiol. 48:77-84(2003).
RN [3]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
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]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-398, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RA Covarrubias A.S., Larsson A.M., Jones T.A., Bergfors T., Mowbray S.L.,
RA Unge T.;
RT "Structure and biochemical function studies of Mycobacterium tuberculosis
RT essential protein Rv3778c.";
RL Submitted (JAN-2010) to the PDB data bank.
CC -!- FUNCTION: Is essential for optimal growth.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene display impaired growth.
CC {ECO:0000269|PubMed:12657046}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved Lysine residue that is involved in
CC covalent pyridoxal phosphate binding in other members of the family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP46607.1; -; Genomic_DNA.
DR PIR; F70695; F70695.
DR RefSeq; NP_218295.1; NC_000962.3.
DR RefSeq; WP_003420595.1; NZ_NVQJ01000009.1.
DR PDB; 3CAI; X-ray; 1.80 A; A/B=2-398.
DR PDBsum; 3CAI; -.
DR AlphaFoldDB; P9WQ67; -.
DR SMR; P9WQ67; -.
DR STRING; 83332.Rv3778c; -.
DR PaxDb; P9WQ67; -.
DR DNASU; 886116; -.
DR GeneID; 886116; -.
DR KEGG; mtu:Rv3778c; -.
DR TubercuList; Rv3778c; -.
DR eggNOG; COG0520; Bacteria.
DR OMA; PYRLIDI; -.
DR PhylomeDB; P9WQ67; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0016740; F:transferase activity; IEA:UniProt.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR011340; Cys_dSase-rel.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01976; am_tr_V_VC1184; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome.
FT CHAIN 1..398
FT /note="Uncharacterized protein Rv3778c"
FT /id="PRO_0000415516"
FT HELIX 5..10
FT /evidence="ECO:0007829|PDB:3CAI"
FT TURN 13..16
FT /evidence="ECO:0007829|PDB:3CAI"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:3CAI"
FT HELIX 32..44
FT /evidence="ECO:0007829|PDB:3CAI"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:3CAI"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:3CAI"
FT HELIX 54..74
FT /evidence="ECO:0007829|PDB:3CAI"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:3CAI"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:3CAI"
FT HELIX 87..97
FT /evidence="ECO:0007829|PDB:3CAI"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:3CAI"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:3CAI"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:3CAI"
FT HELIX 120..129
FT /evidence="ECO:0007829|PDB:3CAI"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:3CAI"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:3CAI"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:3CAI"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:3CAI"
FT STRAND 158..166
FT /evidence="ECO:0007829|PDB:3CAI"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:3CAI"
FT HELIX 177..185
FT /evidence="ECO:0007829|PDB:3CAI"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:3CAI"
FT TURN 195..200
FT /evidence="ECO:0007829|PDB:3CAI"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:3CAI"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:3CAI"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:3CAI"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:3CAI"
FT HELIX 233..237
FT /evidence="ECO:0007829|PDB:3CAI"
FT HELIX 250..254
FT /evidence="ECO:0007829|PDB:3CAI"
FT HELIX 261..275
FT /evidence="ECO:0007829|PDB:3CAI"
FT HELIX 285..312
FT /evidence="ECO:0007829|PDB:3CAI"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:3CAI"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:3CAI"
FT STRAND 328..334
FT /evidence="ECO:0007829|PDB:3CAI"
FT HELIX 339..348
FT /evidence="ECO:0007829|PDB:3CAI"
FT HELIX 360..364
FT /evidence="ECO:0007829|PDB:3CAI"
FT TURN 365..371
FT /evidence="ECO:0007829|PDB:3CAI"
FT STRAND 374..377
FT /evidence="ECO:0007829|PDB:3CAI"
FT HELIX 384..395
FT /evidence="ECO:0007829|PDB:3CAI"
SQ SEQUENCE 398 AA; 41852 MW; 38ABAB9B1B9D1EA4 CRC64;
MAYDVARVRG LHPSLGDGWV HFDAPAGMLI PDSVATTVST AFRRSGASTV GAHPSARRSA
AVLDAAREAV ADLVNADPGG VVLGADRAVL LSLLAEASSS RAGLGYEVIV SRLDDEANIA
PWLRAAHRYG AKVKWAEVDI ETGELPTWQW ESLISKSTRL VAVNSASGTL GGVTDLRAMT
KLVHDVGALV VVDHSAAAPY RLLDIRETDA DVVTVNAHAW GGPPIGAMVF RDPSVMNSFG
SVSTNPYATG PARLEIGVHQ FGLLAGVVAS IEYLAALDES ARGSRRERLA VSMQSADAYL
NRVFDYLMVS LRSLPLVMLI GRPEAQIPVV SFAVHKVPAD RVVQRLADNG ILAIANTGSR
VLDVLGVNDV GGAVTVGLAH YSTMAEVDQL VRALASLG
