ID   Q8YDN4_BRUME            Unreviewed;       271 AA.
AC   Q8YDN4;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 127.
DE   SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:AAL53382.1};
DE            EC=1.2.1.3 {ECO:0000313|EMBL:AAL53382.1};
GN   OrderedLocusNames=BMEII0141 {ECO:0000313|EMBL:AAL53382.1};
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914 {ECO:0000313|EMBL:AAL53382.1, ECO:0000313|Proteomes:UP000000419};
RN   [1] {ECO:0000313|EMBL:AAL53382.1, ECO:0000313|Proteomes:UP000000419}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094
RC   {ECO:0000313|Proteomes:UP000000419};
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.J.,
RA   Haselkorn R., Kyrpides N., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; AE008918; AAL53382.1; -; Genomic_DNA.
DR   PIR; AC3527; AC3527.
DR   AlphaFoldDB; Q8YDN4; -.
DR   KEGG; bme:BMEII0141; -.
DR   KEGG; bmel:DK63_3104; -.
DR   PATRIC; fig|224914.52.peg.3250; -.
DR   eggNOG; COG1012; Bacteria.
DR   PhylomeDB; Q8YDN4; -.
DR   Proteomes; UP000000419; Chromosome II.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   PANTHER; PTHR11699:SF263; ALDEHYDE DEHYDROGENASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345}.
FT   DOMAIN          5..271
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   271 AA;  29158 MW;  93E2C81FDFAB93B3 CRC64;
     MEVVQDDNEG RVEIHRKPIG VTGSITPWNW PVMIACWHII PAVRTGNTVV IKPSPLTPLS
     TIRLVEIINE VLPAGVVNVV TGENSIGAAL SAHPGIAKMT FTGSTETGRK IMASAAATLK
     RLTLELGGND AGIVLPDADP ARIAEGLFWG AFINSGQTCA ALKRLYVHDH IYDDVCRHLT
     EYAANIIIGD GLDEKSVLGL VQNAMQFNKV RELVDDARAK GARILIGGEA AEGPGYFYPI
     TLVADIDNGT RLVDEEQFGP VLPIIRYSDI D
//