Y3778_MYCTO
ID Y3778_MYCTO Reviewed; 398 AA.
AC P9WQ66; 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 35.
DE RecName: Full=Uncharacterized protein MT3887;
GN OrderedLocusNames=MT3887;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Is essential for optimal growth. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000516; AAK48252.1; -; Genomic_DNA.
DR PIR; F70695; F70695.
DR RefSeq; WP_003420595.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WQ66; -.
DR SMR; P9WQ66; -.
DR EnsemblBacteria; AAK48252; AAK48252; MT3887.
DR KEGG; mtc:MT3887; -.
DR PATRIC; fig|83331.31.peg.4182; -.
DR HOGENOM; CLU_003433_2_2_11; -.
DR Proteomes; UP000001020; Chromosome.
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 3: Inferred from homology;
FT CHAIN 1..398
FT /note="Uncharacterized protein MT3887"
FT /id="PRO_0000426829"
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