ID A0A061ILB4_CRIGR Unreviewed; 374 AA.
AC A0A061ILB4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
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|Ensembl:ENSCGRP00001000544.1,
GN ECO:0000313|RefSeq:XP_027251617.1};
GN ORFNames=H671_1g3008 {ECO:0000313|EMBL:ERE88509.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:ERE88509.1, ECO:0000313|Proteomes:UP000030759};
RN [1] {ECO:0000313|Proteomes:UP000030759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17A/GY {ECO:0000313|Proteomes:UP000030759};
RX PubMed=23929341; DOI=10.1038/nbt.2645;
RA Brinkrolf K., Rupp O., Laux H., Kollin F., Ernst W., Linke B., Kofler R.,
RA Romand S., Hesse F., Budach W.E., Galosy S., Muller D., Noll T.,
RA Wienberg J., Jostock T., Leonard M., Grillari J., Tauch A., Goesmann A.,
RA Helk B., Mott J.E., Puhler A., Borth N.;
RT "Chinese hamster genome sequenced from sorted chromosomes.";
RL Nat. Biotechnol. 31:694-695(2013).
RN [2] {ECO:0000313|EMBL:ERE88509.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=17A/GY {ECO:0000313|EMBL:ERE88509.1};
RA Brinkrolf K., Rupp O., Laux H., Kollin F., Ernst W., Linke B., Kofler R.,
RA Romand S., Hesse F., Budach W.E., Galosy S., Muller D., Noll T.,
RA Wienberg J., Jostock T., Leonard M., Grillari J., Tauch A., Goesmann A.,
RA Helk B., Mott J.E., Puehler A., Borth N.;
RT "Chinese hamster genome sequenced from sorted chromosomes.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSCGRP00001000544.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [4] {ECO:0000313|RefSeq:XP_027251617.1}
RP IDENTIFICATION.
RC STRAIN=17A/GY {ECO:0000313|RefSeq:XP_027251617.1};
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_027251617.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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; KE665759; ERE88509.1; -; Genomic_DNA.
DR RefSeq; XP_007605859.1; XM_007607669.2.
DR RefSeq; XP_007629006.1; XM_007630816.2.
DR RefSeq; XP_027251617.1; XM_027395816.2.
DR Ensembl; ENSCGRT00001000568.1; ENSCGRP00001000544.1; ENSCGRG00001000437.1.
DR Ensembl; ENSCGRT00001000580.1; ENSCGRP00001000556.1; ENSCGRG00001000437.1.
DR GeneID; 100767929; -.
DR KEGG; cge:100767929; -.
DR CTD; 128; -.
DR GeneTree; ENSGT00940000155196; -.
DR OMA; IKGRSEM; -.
DR OrthoDB; 1077476at2759; -.
DR Proteomes; UP000030759; Unassembled WGS sequence.
DR Proteomes; UP000694386; Unplaced.
DR Proteomes; UP001108280; Chromosome 1.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0005504; F:fatty acid binding; IEA:Ensembl.
DR GO; GO:0018467; F:formaldehyde dehydrogenase activity; IEA:Ensembl.
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:Ensembl.
DR GO; GO:0006069; P:ethanol oxidation; IEA:InterPro.
DR GO; GO:0010430; P:fatty acid omega-oxidation; IEA:Ensembl.
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:0051775; P:response to redox state; 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 3: Inferred from homology;
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; 39651 MW; B5EE562B0E53AEB9 CRC64;
MANQVIRCKA AVAWEAGKPL SIEEVEVAPP KAHEVRIKII ATAVCHTDAY TLSGADPEGC
FPVILGHEGA GIVESVGEGV TRVKAGDTVI PLYVPQCGEC KFCLNPKTNL CQKIRVTQGK
GLMPDGTTRF TCKGKPLFHF MGTSTFSEYT VVADISVAKI DPSAPLDKVC LLGCGVSTGY
GAAVNTAKVE PGSTCAVFGL GGVGLAVIMG CKVAGASRII GIDINKDKFA KAKEFGATEC
INPQEFNKPI QEVLIEMTDG GVDFSFECIG NVKVMRAALE AAHKGWGVSV VVGVAASGEE
ISTRPFQLVT GRTWKGTAFG GWKSVESVPK LVSEYMSKKI KVDEFVTDNL SFDQINKALD
LMHSGKSIRT VLKL
//
