Y4146_MYCPA
ID Y4146_MYCPA Reviewed; 275 AA.
AC Q73SC8;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Uncharacterized NAD-dependent oxidoreductase MAP_4146;
DE EC=1.-.-.-;
GN OrderedLocusNames=MAP_4146;
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10;
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-275 IN COMPLEX WITH NAD.
RG Seattle structural genomics center for infectious disease (SSGCID);
RT "Crystal structure of a putative carveol dehydrogenase from Mycobacterium
RT paratuberculosis bound to nicotinamide adenine dinucleotide.";
RL Submitted (NOV-2010) to the PDB data bank.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {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; AE016958; AAS06696.1; -; Genomic_DNA.
DR RefSeq; WP_003879429.1; NC_002944.2.
DR PDB; 3PGX; X-ray; 1.85 A; A/B/C/D=2-275.
DR PDBsum; 3PGX; -.
DR AlphaFoldDB; Q73SC8; -.
DR SMR; Q73SC8; -.
DR STRING; 262316.MAP_4146; -.
DR EnsemblBacteria; AAS06696; AAS06696; MAP_4146.
DR KEGG; mpa:MAP_4146; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_1_0_11; -.
DR OMA; NISSMWG; -.
DR BRENDA; 1.1.1.275; 3508.
DR EvolutionaryTrace; Q73SC8; -.
DR Proteomes; UP000000580; Chromosome.
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 InterPro; IPR023985; SDR_subfam_1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR03971; SDR_subfam_1; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..275
FT /note="Uncharacterized NAD-dependent oxidoreductase
FT MAP_4146"
FT /id="PRO_0000416410"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 20..22
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 41..42
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 80..81
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 107
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 206..208
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.2"
FT TURN 7..10
FT /evidence="ECO:0007829|PDB:3PGX"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:3PGX"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:3PGX"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:3PGX"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:3PGX"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:3PGX"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:3PGX"
FT HELIX 84..98
FT /evidence="ECO:0007829|PDB:3PGX"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:3PGX"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:3PGX"
FT HELIX 121..131
FT /evidence="ECO:0007829|PDB:3PGX"
FT HELIX 133..149
FT /evidence="ECO:0007829|PDB:3PGX"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:3PGX"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:3PGX"
FT HELIX 171..191
FT /evidence="ECO:0007829|PDB:3PGX"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:3PGX"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:3PGX"
FT HELIX 213..222
FT /evidence="ECO:0007829|PDB:3PGX"
FT HELIX 224..229
FT /evidence="ECO:0007829|PDB:3PGX"
FT HELIX 243..254
FT /evidence="ECO:0007829|PDB:3PGX"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:3PGX"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:3PGX"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:3PGX"
SQ SEQUENCE 275 AA; 28940 MW; D34B8D31B48B8CA5 CRC64;
MAGQAGSLQG RVAFITGAAR GQGRSHAVRL AAEGADIIAC DICAPVSASV TYAPASPEDL
DETARLVEDQ GRKALTRVLD VRDDAALREL VADGMEQFGR LDVVVANAGV LSWGRVWELT
DEQWDTVIGV NLTGTWRTLR ATVPAMIEAG NGGSIVVVSS SAGLKATPGN GHYSASKHGL
TALTNTLAIE LGEYGIRVNS IHPYSVETPM IEPEAMMEIF ARHPSFVHSF PPMPVQPNGF
MTADEVADVV AWLAGDGSGT LTGTQIPVDK GALKY