LinkDB: H2QXA8_PANTR G2HHH5_PANTR
Original site: H2QXA8_PANTR G2HHH5_PANTR
ID H2QXA8_PANTR Unreviewed; 517 AA. AC H2QXA8; A0A2J8QRI8; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAR-2024, entry version 61. DE RecName: Full=Aldehyde dehydrogenase X, mitochondrial {ECO:0000256|ARBA:ARBA00040048}; DE EC=1.2.1.3 {ECO:0000256|ARBA:ARBA00024226}; DE AltName: Full=Aldehyde dehydrogenase family 1 member B1 {ECO:0000256|ARBA:ARBA00041645}; GN Name=ALDH1B1 {ECO:0000313|EMBL:JAA05233.1, GN ECO:0000313|Ensembl:ENSPTRP00000035841.1, ECO:0000313|VGNC:VGNC:4609}; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pan. OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000035841.1, ECO:0000313|Proteomes:UP000002277}; RN [1] {ECO:0000313|Ensembl:ENSPTRP00000035841.1, ECO:0000313|Proteomes:UP000002277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16136131; DOI=10.1038/nature04072; RG Chimpanzee sequencing and analysis consortium; RT "Initial sequence of the chimpanzee genome and comparison with the human RT genome."; RL Nature 437:69-87(2005). RN [2] {ECO:0000313|EMBL:JAA05233.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA05233.1}, Skeletal muscle RC {ECO:0000313|EMBL:JAA35772.1}, Skin {ECO:0000313|EMBL:JAA24361.1}, and RC Smooth vascular {ECO:0000313|EMBL:JAA11560.1}; RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.; RT "De novo assembly of the reference chimpanzee transcriptome from NextGen RT mRNA sequences."; RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSPTRP00000035841.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH; CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; EC=1.2.1.3; CC Evidence={ECO:0000256|ARBA:ARBA00024149}; CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol: CC step 2/2. {ECO:0000256|ARBA:ARBA00037885}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix CC {ECO:0000256|ARBA:ARBA00004305}. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}. 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; AACZ04033376; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; GABC01006105; JAA05233.1; -; mRNA. DR EMBL; GABF01010585; JAA11560.1; -; mRNA. DR EMBL; GABD01008739; JAA24361.1; -; mRNA. DR EMBL; GABE01008967; JAA35772.1; -; mRNA. DR RefSeq; XP_009454522.1; XM_009456247.2. DR STRING; 9598.ENSPTRP00000035841; -. DR PaxDb; 9598-ENSPTRP00000035841; -. DR Ensembl; ENSPTRT00000038769.2; ENSPTRP00000035841.1; ENSPTRG00000020956.2. DR GeneID; 464931; -. DR CTD; 219; -. DR VGNC; VGNC:4609; ALDH1B1. DR eggNOG; KOG2450; Eukaryota. DR GeneTree; ENSGT00940000162530; -. DR HOGENOM; CLU_005391_0_2_1; -. DR OMA; WVNRYGR; -. DR OrthoDB; 2291791at2759; -. DR TreeFam; TF300455; -. DR Proteomes; UP000002277; Chromosome 9. DR Bgee; ENSPTRG00000020956; Expressed in liver and 19 other cell types or tissues. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl. DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central. DR CDD; cd07141; ALDH_F1AB_F2_RALDH1; 1. 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:SF207; ALDEHYDE DEHYDROGENASE X, MITOCHONDRIAL; 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 2: Evidence at transcript level; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU003345}; KW Reference proteome {ECO:0000313|Proteomes:UP000002277}. FT DOMAIN 45..508 FT /note="Aldehyde dehydrogenase" FT /evidence="ECO:0000259|Pfam:PF00171" FT ACT_SITE 285 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007" SQ SEQUENCE 517 AA; 57276 MW; 519E165467B1A798 CRC64; MLRFLAPRLL SLQGRTAHYS SAAALPSPIL NPDIPYNQLF INNEWQDAVS KKTFPTVNPT TGEVIGHVAE GDRADVDRAV KAAREAFRLG SPWRRMDASE RGRLLNRLAD LVERDRVYLA SLETLDNGKP FQESYALDLD EVIKVYRYFA GWADKWHGKT IPMDGQHFCF TRHEPVGVCG QIIPWNFPLV MQGWKLAPAL ATGNTVVMKV AEQTPLSALY LASLIKEAGF PPGVVNIITG YGPTAGAAIA QHMDVDKVAF TGSTEVGHLI QKAAGDSNLK RVTLELGGKS PSIVLADADM EHAVEQCHEA LFFNMGQCCC AGSRTFVEES IYNEFLERTV EKAKQRKVGN PFELDTQQGP QVDKEQFERV LGYIQLGQKE GAKLLCGGER FGERGFFIKP TVFGGVQDDM RIAKEEIFGP VQPLFKFKKI EEVIERANNT RYGLAAAVFT RDLDKAMYFT QALQAGTVWV NTYNIVTCHT PFGGFKESGN GRELGEDGLK AYTEVKTVTI KVPQKNS //
ID G2HHH5_PANTR Unreviewed; 517 AA. AC G2HHH5; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAR-2024, entry version 36. DE RecName: Full=Aldehyde dehydrogenase X, mitochondrial {ECO:0000256|ARBA:ARBA00040048}; DE EC=1.2.1.3 {ECO:0000256|ARBA:ARBA00024226}; DE AltName: Full=Aldehyde dehydrogenase family 1 member B1 {ECO:0000256|ARBA:ARBA00041645}; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pan. OX NCBI_TaxID=9598 {ECO:0000313|EMBL:BAK63183.1}; RN [1] {ECO:0000313|EMBL:BAK63183.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Testis {ECO:0000313|EMBL:BAK63183.1}; RX PubMed=21484476; DOI=10.1007/s10142-011-0220-9; RA Kim R.N., Kim D.W., Choi S.H., Chae S.H., Nam S.H., Kim D.W., Kim A., RA Kang A., Park K.H., Lee Y.S., Hirai M., Suzuki Y., Sugano S., Hashimoto K., RA Kim D.S., Park H.S.; RT "Major chimpanzee-specific structural changes in sperm development- RT associated genes."; RL Funct. Integr. Genomics 11:507-517(2011). CC -!- CATALYTIC ACTIVITY: CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH; CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; EC=1.2.1.3; CC Evidence={ECO:0000256|ARBA:ARBA00024149}; CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol: CC step 2/2. {ECO:0000256|ARBA:ARBA00037885}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix CC {ECO:0000256|ARBA:ARBA00004305}. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}. 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; AK306189; BAK63183.1; -; mRNA. DR RefSeq; NP_001266946.1; NM_001280017.1. DR AlphaFoldDB; G2HHH5; -. DR GeneID; 464931; -. DR KEGG; ptr:464931; -. DR CTD; 219; -. DR OrthoDB; 2291791at2759; -. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro. DR CDD; cd07141; ALDH_F1AB_F2_RALDH1; 1. 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:SF207; ALDEHYDE DEHYDROGENASE X, MITOCHONDRIAL; 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 2: Evidence at transcript level; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU003345}. FT DOMAIN 45..508 FT /note="Aldehyde dehydrogenase" FT /evidence="ECO:0000259|Pfam:PF00171" FT ACT_SITE 285 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007" SQ SEQUENCE 517 AA; 57213 MW; A28B44E7FA3C1FD6 CRC64; MLRFLAPRLL SLQGRTARYS SVAALPSPIL NPDIPYNQLF INNEWQDAVS KKTFPTVNPT TGEVIGHVAE GDRADVDRAV KAAREAFRLG SPWRRMDASE RGRLLNRLAD LVERDRVYLA SLETLDNGKP FQESYALDLD EVIKVYRYFA GWADKCHGKT IPMDGQHFCF TRHEPVGVCG QIIPWNFPLV MQGWKLAPAL ATGSTVVMKV AEQTPLSALY LASLIKEAGF PPGVVNIITG YGPTAGAAIA QHMDVDKVAF TGSTEVGHLI QKAAGDSNLK RVTLELGGKS PSIVLADADM EHAVEQCHEA LFFNMGQCCC AGSRTFVEES IYNEFLERTV EKAKQRKVGN PFELDTQQGP QVDKEQFERV LGYIQLGQKE GAKLLCGGER FGERGFFIKP TVFGGVQDDM RIAKEEIFGP VQPLFKFKKI EEVIERANNT RYGLAAAVFT RDLDKAMYFT QALQAGTVWV NTYNIVTCHT PFGGFKESGN GRELGEDGLK AYTEVKTVTI KVPQKNS //