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Database: UniProt/TrEMBL
Entry: I3R908_HALMT
LinkDB: I3R908_HALMT
Original site: I3R908_HALMT 
ID   I3R908_HALMT            Unreviewed;       522 AA.
AC   I3R908;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:AFK20718.1, ECO:0000313|EMBL:AHZ24026.1};
DE            EC=1.2.1.3 {ECO:0000313|EMBL:AFK20718.1};
GN   Name=aldY2 {ECO:0000313|EMBL:AFK20718.1};
GN   OrderedLocusNames=HFX_4023 {ECO:0000313|EMBL:AFK20718.1};
GN   ORFNames=BM92_19690 {ECO:0000313|EMBL:AHZ24026.1}, C439_16888
GN   {ECO:0000313|EMBL:ELZ97612.1}, E6P09_18965
GN   {ECO:0000313|EMBL:QCQ77402.1};
OS   Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS   14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OG   Plasmid HMPLAS3 {ECO:0000313|EMBL:AHZ24026.1,
OG   ECO:0000313|Proteomes:UP000027075},
OG   Plasmid pHM100 {ECO:0000313|EMBL:AFK20718.1,
OG   ECO:0000313|Proteomes:UP000006469}, and
OG   Plasmid pHME132 {ECO:0000313|EMBL:QCQ77402.1,
OG   ECO:0000313|Proteomes:UP000299011}.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=523841 {ECO:0000313|EMBL:AFK20718.1, ECO:0000313|Proteomes:UP000006469};
RN   [1] {ECO:0000313|EMBL:AFK20718.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CGMCC 1.2087 {ECO:0000313|EMBL:AFK20718.1};
RX   PubMed=22247127; DOI=10.1128/AEM.07114-11;
RA   Cai S., Cai L., Liu H., Liu X., Han J., Zhou J., Xiang H.;
RT   "Identification of the haloarchaeal phasin (PhaP) that functions in
RT   polyhydroxyalkanoate accumulation and granule formation in Haloferax
RT   mediterranei.";
RL   Appl. Environ. Microbiol. 78:1946-1952(2012).
RN   [2] {ECO:0000313|EMBL:AFK20718.1, ECO:0000313|Proteomes:UP000006469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
RC   R-4 {ECO:0000313|Proteomes:UP000006469}, and CGMCC 1.2087
RC   {ECO:0000313|EMBL:AFK20718.1};
RC   PLASMID=pHM100 {ECO:0000313|Proteomes:UP000006469};
RX   PubMed=22843593; DOI=10.1128/JB.00880-12;
RA   Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y.,
RA   Zhou J., Hu S., Xiang H.;
RT   "Complete genome sequence of the metabolically versatile halophilic
RT   archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT   hydroxyvalerate) producer.";
RL   J. Bacteriol. 194:4463-4464(2012).
RN   [3] {ECO:0000313|Proteomes:UP000011603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
RC   R-4 {ECO:0000313|Proteomes:UP000011603};
RA   Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA   Eisen J.A., Facciotti M.T.;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:ELZ97612.1, ECO:0000313|Proteomes:UP000011603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33500 {ECO:0000313|EMBL:ELZ97612.1}, and ATCC 33500 / DSM
RC   1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC   {ECO:0000313|Proteomes:UP000011603};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
RN   [5] {ECO:0000313|EMBL:AHZ24026.1, ECO:0000313|Proteomes:UP000027075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33500 {ECO:0000313|EMBL:AHZ24026.1}, and ATCC 33500 / DSM
RC   1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC   {ECO:0000313|Proteomes:UP000027075};
RC   PLASMID=HMPLAS3 {ECO:0000313|EMBL:AHZ24026.1}, and Plasmid HMPLAS3
RC   {ECO:0000313|Proteomes:UP000027075};
RA   Bautista V.;
RT   "Transcriptional profiles of Haloferax mediterranei on the basis of
RT   nitrogen availability.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:AFK20718.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CGMCC 1.2087 {ECO:0000313|EMBL:AFK20718.1};
RC   PLASMID=pHM100 {ECO:0000313|EMBL:AFK20718.1};
RA   Wang L., Yang H., Xiang H.;
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:QCQ77402.1, ECO:0000313|Proteomes:UP000299011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33500 {ECO:0000313|EMBL:QCQ77402.1}, and ATCC 33500 / DSM
RC   1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC   {ECO:0000313|Proteomes:UP000299011};
RC   PLASMID=pHME132 {ECO:0000313|EMBL:QCQ77402.1,
RC   ECO:0000313|Proteomes:UP000299011};
RA   DasSarma S., DasSarma P., DasSarma S., Fomenkov A., Vincze T., Anton B.P.,
RA   Roberts R.J.;
RT   "Methylomes of two halophilic Archaea, Haloarcula marismortui and Haloferax
RT   mediterranei.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP001869; AFK20718.1; -; Genomic_DNA.
DR   EMBL; CP007552; AHZ24026.1; -; Genomic_DNA.
DR   EMBL; AOLO01000014; ELZ97612.1; -; Genomic_DNA.
DR   EMBL; CP039142; QCQ77402.1; -; Genomic_DNA.
DR   RefSeq; WP_004060539.1; NZ_CP039142.1.
DR   AlphaFoldDB; I3R908; -.
DR   GeneID; 40158544; -.
DR   KEGG; hme:HFX_4023; -.
DR   PATRIC; fig|523841.21.peg.3397; -.
DR   HOGENOM; CLU_005391_0_2_2; -.
DR   OrthoDB; 6342at2157; -.
DR   Proteomes; UP000006469; Plasmid pHM100.
DR   Proteomes; UP000011603; Unassembled WGS sequence.
DR   Proteomes; UP000027075; Plasmid HMPLAS3.
DR   Proteomes; UP000299011; Plasmid pHME132.
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:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 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   Oxidoreductase {ECO:0000256|RuleBase:RU003345,
KW   ECO:0000313|EMBL:AFK20718.1}; Plasmid {ECO:0000313|EMBL:AFK20718.1}.
FT   DOMAIN          41..511
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        278
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   522 AA;  56104 MW;  FEF26CD089B2695F CRC64;
     MQDTYFNDTF DIDDAVLERH RTAVESSLER DEYGLLIGSK WVDSEGGEEG VAIDPTTGES
     LATFQVGTAA DVDRAVEAAR NAYEGNWGQL SPRQRGEKLE EIADRLAERK TELAKIETLE
     AGKPNLHSRF VDIEILVEQF RHFAAVARTA DTGRVVPTDD EKHVVTKREP YGVVGAISAW
     NFPAMFVAWK LGPALAAGNA VVFKPSSKAV LATLEIADVC DTVLPTGTVN VVTGAGSVVG
     NAISQHDGID KVTLTGSKAA GTATLEGAAD TITPVSLELG GKSPNIVFPD TDLEQALEGT
     IVSIFFNSGQ QCTAGSRLFL HEDIKDEFLD MLRERIDELT VGDPLSPQTD IGPMIDHDHA
     EQVTGYISRA IEDGARPLVG DDVDEVDAGG EASDTAGAPF VQPTVLTGVD DSAEVACDEV
     FGPVLSVFEW SERDEVIERA NDTRFGLAAG VWTQDLETAH DVADELKAGT VWVNTYDDML
     DPAPHGGYKE SGMGRELSEE ALDDYSRTKS VKMNFGEVLK IG
//
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