ID   Q6IRT1_HUMAN            Unreviewed;       374 AA.
AC   Q6IRT1; A0A024RDI2;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 2.
DT   27-MAR-2024, entry version 169.
DE   RecName: Full=S-(hydroxymethyl)glutathione dehydrogenase {ECO:0000256|RuleBase:RU362016};
DE            EC=1.1.1.284 {ECO:0000256|RuleBase:RU362016};
GN   Name=ADH5 {ECO:0000313|EMBL:AAH70491.2};
GN   Synonyms=HEL-S-60p {ECO:0000313|EMBL:ACV87211.1};
GN   ORFNames=hCG_41483 {ECO:0000313|EMBL:EAX06084.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:AAH70491.2};
RN   [1] {ECO:0000313|EMBL:EAX06084.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11181995; DOI=10.1126/science.1058040;
RA   Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G.,
RA   Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P.,
RA   Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.,
RA   Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J.,
RA   Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J.,
RA   McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C.,
RA   Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M.,
RA   Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C.,
RA   Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K.,
RA   Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R.,
RA   Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K.,
RA   Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P.,
RA   Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y.,
RA   Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N.,
RA   Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B.,
RA   Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J.,
RA   Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W.,
RA   Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S.,
RA   Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T.,
RA   Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I.,
RA   Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L.,
RA   Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L.,
RA   Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C.,
RA   Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C.,
RA   Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D.,
RA   McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B.,
RA   Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M.,
RA   Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C.,
RA   Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S.,
RA   Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S.,
RA   Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R.,
RA   Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B.,
RA   Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S.,
RA   Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S.,
RA   Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J.,
RA   Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M.,
RA   Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S.,
RA   Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M.,
RA   Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J.,
RA   Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J.,
RA   Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N.,
RA   Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J.,
RA   Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E.,
RA   Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.;
RT   "The sequence of the human genome.";
RL   Science 291:1304-1351(2001).
RN   [2] {ECO:0000313|EMBL:AAH70491.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skin {ECO:0000313|EMBL:AAH70491.2};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3] {ECO:0000313|EMBL:EAX06084.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:BAG35285.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Amygdala {ECO:0000313|EMBL:BAG35285.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y.,
RA   Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R.,
RA   Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N.,
RA   Isogai T.;
RT   "NEDO functional analysis of protein and research application project.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:ACV87211.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Sahoo P.;
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + NAD(+) = 20-
CC         oxo-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + NADH;
CC         Xref=Rhea:RHEA:39799, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:76624, ChEBI:CHEBI:76645;
CC         Evidence={ECO:0000256|ARBA:ARBA00000011};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39800;
CC         Evidence={ECO:0000256|ARBA:ARBA00000011};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=20-oxo-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H2O + NAD(+) =
CC         (5Z,8Z,11Z,14Z)-eicosatetraenedioate + 2 H(+) + NADH;
CC         Xref=Rhea:RHEA:39803, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:76645,
CC         ChEBI:CHEBI:76647; Evidence={ECO:0000256|ARBA:ARBA00000576};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39804;
CC         Evidence={ECO:0000256|ARBA:ARBA00000576};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + S-(hydroxymethyl)glutathione = H(+) + NADH + S-
CC         formylglutathione; Xref=Rhea:RHEA:19985, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57688, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58758; EC=1.1.1.284;
CC         Evidence={ECO:0000256|ARBA:ARBA00001030,
CC         ECO:0000256|RuleBase:RU362016};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + S-(hydroxymethyl)glutathione = H(+) + NADPH + S-
CC         formylglutathione; Xref=Rhea:RHEA:19981, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57688, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:58758; EC=1.1.1.284;
CC         Evidence={ECO:0000256|ARBA:ARBA00001646};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC         Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001146};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC         Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC         ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000781};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU362016};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Class-III subfamily. {ECO:0000256|ARBA:ARBA00010902,
CC       ECO:0000256|RuleBase:RU362016}.
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DR   EMBL; BC070491; AAH70491.2; -; mRNA.
DR   EMBL; GQ472236; ACV87211.1; -; mRNA.
DR   EMBL; AK312367; BAG35285.1; -; mRNA.
DR   EMBL; CH471057; EAX06084.1; -; Genomic_DNA.
DR   RefSeq; NP_000662.3; NM_000671.4.
DR   SMR; Q6IRT1; -.
DR   Antibodypedia; 25845; 502 antibodies from 37 providers.
DR   DNASU; 128; -.
DR   GeneID; 128; -.
DR   KEGG; hsa:128; -.
DR   UCSC; uc003hui.5; human.
DR   CTD; 128; -.
DR   PharmGKB; PA24574; -.
DR   VEuPathDB; HostDB:ENSG00000197894; -.
DR   HOGENOM; CLU_026673_14_0_1; -.
DR   OMA; IKGRSEM; -.
DR   OrthoDB; 1077476at2759; -.
DR   BioGRID-ORCS; 128; 121 hits in 1159 CRISPR screens.
DR   ChiTaRS; ADH5; human.
DR   GenomeRNAi; 128; -.
DR   ExpressionAtlas; Q6IRT1; baseline and differential.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0106322; F:S-(hydroxymethyl)glutathione dehydrogenase NAD activity; IEA:UniProtKB-EC.
DR   GO; GO:0106321; F:S-(hydroxymethyl)glutathione dehydrogenase NADP activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006069; P:ethanol oxidation; IEA:InterPro.
DR   GO; GO:0046294; P:formaldehyde catabolic process; IEA:Ensembl.
DR   GO; GO:0045777; P:positive regulation of blood pressure; IEA:Ensembl.
DR   GO; GO:0003016; P:respiratory system process; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0051409; P:response to nitrosative stress; IEA:Ensembl.
DR   GO; GO:0001523; P:retinoid metabolic process; IEA:Ensembl.
DR   CDD; cd08300; alcohol_DH_class_III; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR014183; ADH_3.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR02818; adh_III_F_hyde; 1.
DR   PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43880:SF4; ALCOHOL DEHYDROGENASE CLASS-3; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; GroES-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding {ECO:0000256|RuleBase:RU362016};
KW   NAD {ECO:0000256|RuleBase:RU362016};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362016}; Zinc {ECO:0000256|RuleBase:RU362016}.
FT   DOMAIN          33..120
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          202..331
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   374 AA;  39724 MW;  F4F823B4A609C952 CRC64;
     MANEVIKCKA AVAWEAGKPL SIEEIEVAPP KAHEVRIKII ATAVCHTDAY TLSGADPEGC
     FPVILGHEGA GIVESVGEGV TKLKAGDTVI PLYIPQCGEC KFCLNPKTNL CQKIRVTQGK
     GLMPDGTSRF TCKGKTILHY MGTSTFSEYT VVADISVAKI DPLAPLDKVC LLGCGISTGY
     GAAVNTAKLE PGSVCAVFGL GGVGLAVIMG CKVAGASRII GVDINKDKFA RAKEFGATEC
     INPQDFSKPI QEVLIEMTDG GVDYSFECIG NVKVMRAALE ACHKGWGVSV VVGVAASGEE
     IATRPFQLVT GRTWKGTAFG GWKSVESVPK LVSEYMSKKI KVDEFVTHNL SFDEINKAFE
     LMHSGKSIRT VVKI
//