Y2971_MYCTU
ID Y2971_MYCTU Reviewed; 282 AA.
AC P9WQA5; L0TBF0; P95124; Q7D6C1;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Uncharacterized oxidoreductase Rv2971;
DE EC=1.-.-.-;
GN OrderedLocusNames=Rv2971;
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].
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).
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP45776.1; -; Genomic_DNA.
DR PIR; H70671; H70671.
DR RefSeq; NP_217487.1; NC_000962.3.
DR RefSeq; WP_003899563.1; NZ_NVQJ01000015.1.
DR PDB; 4OTK; X-ray; 1.60 A; A=2-282.
DR PDBsum; 4OTK; -.
DR AlphaFoldDB; P9WQA5; -.
DR SMR; P9WQA5; -.
DR STRING; 83332.Rv2971; -.
DR PaxDb; P9WQA5; -.
DR DNASU; 887275; -.
DR GeneID; 887275; -.
DR KEGG; mtu:Rv2971; -.
DR TubercuList; Rv2971; -.
DR eggNOG; COG0656; Bacteria.
DR OMA; KLWPTDQ; -.
DR PhylomeDB; P9WQA5; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR PANTHER; PTHR43827; PTHR43827; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Oxidoreductase; Reference proteome.
FT CHAIN 1..282
FT /note="Uncharacterized oxidoreductase Rv2971"
FT /id="PRO_0000380747"
FT ACT_SITE 57
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 195..247
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:4OTK"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:4OTK"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:4OTK"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:4OTK"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:4OTK"
FT HELIX 60..69
FT /evidence="ECO:0007829|PDB:4OTK"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:4OTK"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:4OTK"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:4OTK"
FT HELIX 90..104
FT /evidence="ECO:0007829|PDB:4OTK"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:4OTK"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:4OTK"
FT HELIX 124..136
FT /evidence="ECO:0007829|PDB:4OTK"
FT STRAND 139..147
FT /evidence="ECO:0007829|PDB:4OTK"
FT HELIX 150..160
FT /evidence="ECO:0007829|PDB:4OTK"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:4OTK"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:4OTK"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:4OTK"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:4OTK"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:4OTK"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:4OTK"
FT HELIX 219..229
FT /evidence="ECO:0007829|PDB:4OTK"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:4OTK"
FT HELIX 241..248
FT /evidence="ECO:0007829|PDB:4OTK"
FT HELIX 257..264
FT /evidence="ECO:0007829|PDB:4OTK"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:4OTK"
SQ SEQUENCE 282 AA; 30364 MW; DA316780633D7E60 CRC64;
MTGESGAAAA PSITLNDEHT MPVLGLGVAE LSDDETERAV SAALEIGCRL IDTAYAYGNE
AAVGRAIAAS GVAREELFVT TKLATPDQGF TRSQEACRAS LDRLGLDYVD LYLIHWPAPP
VGKYVDAWGG MIQSRGEGHA RSIGVSNFTA ENIENLIDLT FVTPAVNQIE LHPLLNQDEL
RKANAQHTVV TQSYCPLALG RLLDNPTVTS IASEYVKTPA QVLLRWNLQL GNAVVVRSAR
PERIASNFDV FDFELAAEHM DALGGLNDGT RVREDPLTYA GT
