Y432_LISMO
ID Y432_LISMO Reviewed; 248 AA.
AC P25145;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Uncharacterized oxidoreductase Lmo0432;
DE EC=1.-.-.-;
DE AltName: Full=ORFA;
GN OrderedLocusNames=lmo0432;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EGD / Serovar 1/2a;
RX PubMed=1905979; DOI=10.1016/0092-8674(91)90009-n;
RA Gaillard J.-L., Berche P., Frehel C., Gouin E., Cossart P.;
RT "Entry of L. monocytogenes into cells is mediated by internalin, a repeat
RT protein reminiscent of surface antigens from Gram-positive cocci.";
RL Cell 65:1127-1141(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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; M67471; AAA25288.1; -; Genomic_DNA.
DR EMBL; AL591975; CAC98511.1; -; Genomic_DNA.
DR PIR; AI1128; AI1128.
DR PIR; B39930; B39930.
DR RefSeq; NP_463961.1; NC_003210.1.
DR RefSeq; WP_009931125.1; NZ_CP023861.1.
DR AlphaFoldDB; P25145; -.
DR SMR; P25145; -.
DR STRING; 169963.lmo0432; -.
DR PaxDb; P25145; -.
DR EnsemblBacteria; CAC98511; CAC98511; CAC98511.
DR GeneID; 985147; -.
DR KEGG; lmo:lmo0432; -.
DR PATRIC; fig|169963.11.peg.445; -.
DR eggNOG; COG4221; Bacteria.
DR HOGENOM; CLU_010194_2_10_9; -.
DR OMA; EWEQMID; -.
DR PhylomeDB; P25145; -.
DR BioCyc; LMON169963:LMO0432-MON; -.
DR Proteomes; UP000000817; 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 Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..248
FT /note="Uncharacterized oxidoreductase Lmo0432"
FT /id="PRO_0000054883"
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 9..33
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 48
FT /note="T -> I (in Ref. 1; AAA25288)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="V -> A (in Ref. 1; AAA25288)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 26821 MW; 50262487D29FD935 CRC64;
MTIKNKVIII TGASSGIGKA TALLLAEKGA KLVLAARRVE KLEKIVQTIK ANSGEAIFAK
TDVTKREDNK KLVELAIERY GKVDAIFLNA GIMPNSPLSA LKEDEWEQMI DINIKGVLNG
IAAVLPSFIA QKSGHIIATS SVAGLKAYPG GAVYGATKWA VRDLMEVLRM ESAQEGTNIR
TVTIYPAAIN TELLETITDK ETEQGMTSLY KQYGITPDRI ASIVAYAIDQ PEDVNVNEFT
VGPTSQPW