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Database: UniProt
Entry: Y0148_MYCTU
LinkDB: Y0148_MYCTU
Original site: Y0148_MYCTU 
ID   Y0148_MYCTU             Reviewed;         286 AA.
AC   P96825; L0T4I0;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 3.
DT   27-MAR-2024, entry version 127.
DE   RecName: Full=Putative short-chain type dehydrogenase/reductase Rv0148;
DE            EC=1.1.1.-;
GN   OrderedLocusNames=Rv0148;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; 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   PUPYLATION AT LYS-280, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=20066036; DOI=10.1371/journal.pone.0008589;
RA   Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
RA   Gygi S.P., Darwin K.H.;
RT   "Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium
RT   tuberculosis.";
RL   PLoS ONE 5:E8589-E8589(2010).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011445;
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   -!- PTM: Pupylated at Lys-280 by the prokaryotic ubiquitin-like protein
CC       Pup, which probably leads to its degradation by the proteasome.
CC       {ECO:0000269|PubMed:20066036}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP42873.1; -; Genomic_DNA.
DR   PIR; G70617; G70617.
DR   RefSeq; NP_214662.1; NC_000962.3.
DR   RefSeq; WP_003400979.1; NZ_NVQJ01000001.1.
DR   AlphaFoldDB; P96825; -.
DR   SMR; P96825; -.
DR   STRING; 83332.Rv0148; -.
DR   PaxDb; 83332-Rv0148; -.
DR   DNASU; 886845; -.
DR   GeneID; 45424114; -.
DR   GeneID; 886845; -.
DR   KEGG; mtu:Rv0148; -.
DR   TubercuList; Rv0148; -.
DR   eggNOG; COG1028; Bacteria.
DR   InParanoid; P96825; -.
DR   OrthoDB; 9808187at2; -.
DR   PhylomeDB; P96825; -.
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   GO; GO:0070490; P:protein pupylation; IDA:UniProtKB.
DR   CDD; cd05353; hydroxyacyl-CoA-like_DH_SDR_c-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR45024; DEHYDROGENASES, SHORT CHAIN; 1.
DR   PANTHER; PTHR45024:SF2; SCP2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Isopeptide bond; Oxidoreductase; Reference proteome; Ubl conjugation.
FT   CHAIN           1..286
FT                   /note="Putative short-chain type dehydrogenase/reductase
FT                   Rv0148"
FT                   /id="PRO_0000395884"
FT   ACT_SITE        164
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         11..35
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        280
FT                   /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT                   with Q-Cter in protein Pup)"
FT                   /evidence="ECO:0000269|PubMed:20066036"
SQ   SEQUENCE   286 AA;  29779 MW;  84D8E05D8461BAEF CRC64;
     MPGVQDRVIV VTGAGGGLGR EYALTLAGEG ASVVVNDLGG ARDGTGAGSA MADEVVAEIR
     DKGGRAVANY DSVATEDGAA NIIKTALDEF GAVHGVVSNA GILRDGTFHK MSFENWDAVL
     KVHLYGGYHV LRAAWPHFRE QSYGRVVVAT STSGLFGNFG QTNYGAAKLG LVGLINTLAL
     EGAKYNIHAN ALAPIAATRM TQDILPPEVL EKLTPEFVAP VVAYLCTEEC ADNASVYVVG
     GGKVQRVALF GNDGANFDKP PSVQDVAARW AEITDLSGAK IAGFKL
//
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