Y1144_MYCTU
ID Y1144_MYCTU Reviewed; 250 AA.
AC P9WGQ7; L0T7F6; O06544; Q7D8R8;
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 Rv1144;
DE EC=1.-.-.-;
GN OrderedLocusNames=Rv1144;
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 short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43899.1; -; Genomic_DNA.
DR PIR; A70554; A70554.
DR RefSeq; NP_215660.1; NC_000962.3.
DR RefSeq; WP_003405961.1; NZ_NVQJ01000021.1.
DR PDB; 6UJK; X-ray; 1.20 A; A/B=1-250.
DR PDBsum; 6UJK; -.
DR AlphaFoldDB; P9WGQ7; -.
DR SMR; P9WGQ7; -.
DR STRING; 83332.Rv1144; -.
DR PaxDb; P9WGQ7; -.
DR DNASU; 885932; -.
DR GeneID; 45425117; -.
DR GeneID; 885932; -.
DR KEGG; mtu:Rv1144; -.
DR TubercuList; Rv1144; -.
DR eggNOG; COG1028; Bacteria.
DR OMA; QGIRVCT; -.
DR PhylomeDB; P9WGQ7; -.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Oxidoreductase; Reference proteome.
FT CHAIN 1..250
FT /note="Uncharacterized oxidoreductase Rv1144"
FT /id="PRO_0000415506"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 56
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 57
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 82
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 160
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 189
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT BINDING 191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q99714"
FT TURN 1..5
FT /evidence="ECO:0007829|PDB:6UJK"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:6UJK"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:6UJK"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:6UJK"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:6UJK"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:6UJK"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:6UJK"
FT HELIX 60..73
FT /evidence="ECO:0007829|PDB:6UJK"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:6UJK"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:6UJK"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:6UJK"
FT HELIX 112..126
FT /evidence="ECO:0007829|PDB:6UJK"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:6UJK"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:6UJK"
FT HELIX 154..174
FT /evidence="ECO:0007829|PDB:6UJK"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:6UJK"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:6UJK"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:6UJK"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:6UJK"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:6UJK"
FT HELIX 218..230
FT /evidence="ECO:0007829|PDB:6UJK"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:6UJK"
SQ SEQUENCE 250 AA; 25788 MW; 123A1005A12BD6B6 CRC64;
MKTKDAVAVV TGGASGLGLA TTKRLLDAGA QVVVVDLRGD DVVGGLGDRA RFAQADVTDE
AAVSNALELA DSLGPVRVVV NCAGTGNAIR VLSRDGVFPL AAFRKIVDIN LVGTFNVLRL
GAERIAKTEP IGEERGVIIN TASVAAFDGQ IGQAAYSASK GGVVGMTLPI ARDLASKLIR
VVTIAPGLFD TPLLASLPAE AKASLGQQVP HPSRLGNPDE YGALVLHIIE NPMLNGEVIR
LDGAIRMAPR
