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Aralkylamine dehydrogenase light chain (EC 1.4.9.2) (Aromatic amine dehydrogenase) (AADH)

 AAUA_ALCFA              Reviewed;         182 AA.
P84887; Q0VKG6;
15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
15-MAY-2007, sequence version 1.
08-MAY-2019, entry version 65.
RecName: Full=Aralkylamine dehydrogenase light chain;
EC=1.4.9.2;
AltName: Full=Aromatic amine dehydrogenase;
Short=AADH;
Flags: Precursor;
Name=aauA {ECO:0000303|PubMed:17087503};
Alcaligenes faecalis.
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
Alcaligenaceae; Alcaligenes.
NCBI_TaxID=511;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
PubMed=11495996;
Chistoserdov A.Y.;
"Cloning, sequencing and mutagenesis of the genes for aromatic amine
dehydrogenase from Alcaligenes faecalis and evolution of amine
dehydrogenases.";
Microbiology 147:2195-2202(2001).
[2] {ECO:0000305, ECO:0000312|EMBL:CAL23525.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 48-53,
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
AND SUBCELLULAR LOCATION.
STRAIN=ATCC 49677 / NBRC 14479 {ECO:0000269|PubMed:16279953,
ECO:0000312|EMBL:CAL23525.1};
PubMed=16279953; DOI=10.1111/j.1742-4658.2005.04990.x;
Hothi P., Khadra K.A., Combe J.P., Leys D., Scrutton N.S.;
"Tryptophan tryptophylquinone cofactor biogenesis in the aromatic
amine dehydrogenase of Alcaligenes faecalis. Cofactor assembly and
catalytic properties of recombinant enzyme expressed in Paracoccus
denitrificans.";
FEBS J. 272:5894-5909(2005).
[3] {ECO:0000305}
PROTEIN SEQUENCE OF 48-64, FUNCTION, COFACTOR, ACTIVITY REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
STRAIN=ATCC 49677 / NBRC 14479 {ECO:0000269|PubMed:8188594};
PubMed=8188594; DOI=10.1128/jb.176.10.2922-2929.1994;
Govindaraj S., Eisenstein E., Jones L.H., Sanders-Loehr J.,
Chistoserdov A.Y., Davidson V.L., Edwards S.L.;
"Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone
enzyme.";
J. Bacteriol. 176:2922-2929(1994).
[4] {ECO:0000305}
FUNCTION, AND SUBUNIT.
PubMed=7876189; DOI=10.1074/jbc.270.9.4293;
Edwards S.L., Davidson V.L., Hyun Y.-L., Wingfield P.T.;
"Spectroscopic evidence for a common electron transfer pathway for two
tryptophan tryptophylquinone enzymes.";
J. Biol. Chem. 270:4293-4298(1995).
[5] {ECO:0000305}
CATALYTIC ACTIVITY.
STRAIN=ATCC 49677 / NBRC 14479 {ECO:0000269|PubMed:9494080};
PubMed=9494080; DOI=10.1042/bj3301159;
Bishop G.R., Zhu Z., Whitehead T.L., Hicks R.P., Davidson V.L.;
"Identification of reaction products and intermediates of aromatic-
amine dehydrogenase by 15N and 13C NMR.";
Biochem. J. 330:1159-1163(1998).
[6] {ECO:0000305}
SUBCELLULAR LOCATION.
PubMed=10515948;
Zhu Z., Sun D., Davidson V.L.;
"Localization of periplasmic redox proteins of Alcaligenes faecalis by
a modified general method for fractionating Gram-negative bacteria.";
J. Bacteriol. 181:6540-6542(1999).
[7] {ECO:0000305}
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB
AND AZURIN, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
SUBUNIT, AND DISULFIDE BONDS.
STRAIN=ATCC 49677 / NBRC 14479 {ECO:0000269|PubMed:17087503};
PubMed=17087503; DOI=10.1021/bi0612972;
Sukumar N., Chen Z.-W., Ferrari D., Merli A., Rossi G.L.,
Bellamy H.D., Chistoserdov A.Y., Davidson V.L., Mathews F.S.;
"Crystal structure of an electron transfer complex between aromatic
amine dehydrogenase and azurin from Alcaligenes faecalis.";
Biochemistry 45:13500-13510(2006).
[8] {ECO:0000305}
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB
AND SUBSTRATE, FUNCTION, COFACTOR, SUBUNIT, AND DISULFIDE BONDS.
STRAIN=ATCC 49677 / NBRC 14479 {ECO:0000269|PubMed:17005560};
PubMed=17005560; DOI=10.1074/jbc.M605559200;
Roujeinikova A., Scrutton N.S., Leys D.;
"Atomic level insight into the oxidative half-reaction of aromatic
amine dehydrogenase.";
J. Biol. Chem. 281:40264-40272(2006).
[9] {ECO:0000305}
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB
AND SUBSTRATE, FUNCTION, COFACTOR, SUBUNIT, AND DISULFIDE BONDS.
STRAIN=ATCC 49677 / NBRC 14479 {ECO:0000269|PubMed:16614214};
PubMed=16614214; DOI=10.1126/science.1126002;
Masgrau L., Roujeinikova A., Johannissen L.O., Hothi P., Basran J.,
Ranaghan K.E., Mulholland A.J., Sutcliffe M.J., Scrutton N.S.,
Leys D.;
"Atomic description of an enzyme reaction dominated by proton
tunneling.";
Science 312:237-241(2006).
-!- FUNCTION: Oxidizes primary aromatic amines and, more slowly, some
long-chain aliphatic amines, but not methylamine or ethylamine.
Uses azurin as an electron acceptor to transfer electrons from the
reduced tryptophylquinone cofactor. {ECO:0000269|PubMed:11495996,
ECO:0000269|PubMed:16279953, ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503,
ECO:0000269|PubMed:7876189, ECO:0000269|PubMed:8188594}.
-!- CATALYTIC ACTIVITY:
Reaction=an aralkylamine + H2O + 2 oxidized [azurin] = an aromatic
aldehyde + 2 H(+) + NH4(+) + 2 reduced [azurin];
Xref=Rhea:RHEA:47796, Rhea:RHEA-COMP:11034, Rhea:RHEA-
COMP:11035, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:28938, ChEBI:CHEBI:29036, ChEBI:CHEBI:33855,
ChEBI:CHEBI:49552, ChEBI:CHEBI:88332; EC=1.4.9.2;
Evidence={ECO:0000269|PubMed:16279953,
ECO:0000269|PubMed:9494080};
-!- COFACTOR:
Name=tryptophan tryptophylquinone residue; Xref=ChEBI:CHEBI:20251;
Evidence={ECO:0000269|PubMed:16279953,
ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503, ECO:0000269|PubMed:8188594};
Note=Uses a protein-derived tryptophan tryptophylquinone (TTQ)
cofactor. {ECO:0000269|PubMed:16279953,
ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503, ECO:0000269|PubMed:8188594};
-!- ACTIVITY REGULATION: Irreversibly inhibited by phenylhydrazine,
hydroxylamine, semicarbazide, hydrazine and aminoguanidine.
Reversibly inhibited by isonicotinic acid hydrazide (isoniazid)
and isonicotinic acid 2-isopropyl hydrazide (iproniazid).
{ECO:0000269|PubMed:8188594}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Absorption:
Abs(max)=465 nm {ECO:0000269|PubMed:16279953,
ECO:0000269|PubMed:17087503, ECO:0000269|PubMed:8188594};
Note=The above maximum is for the oxidized form. Shows a maximal
peak at 330 nm in the reduced form. These absorption peaks are
for the tryptophylquinone cofactor.
{ECO:0000269|PubMed:16279953, ECO:0000269|PubMed:17087503};
Kinetic parameters:
KM=5.4 uM for tyramine {ECO:0000269|PubMed:16279953,
ECO:0000269|PubMed:17087503, ECO:0000269|PubMed:8188594};
Vmax=17 umol/min/mg enzyme {ECO:0000269|PubMed:16279953,
ECO:0000269|PubMed:17087503, ECO:0000269|PubMed:8188594};
Note=The enzyme is substrate inhibited at high substrate
concentrations (Ki=1.08 mM for tyramine).
{ECO:0000269|PubMed:8188594};
-!- SUBUNIT: Heterotetramer of two light and two heavy chains. Binds
two azurin molecules per heterotetramer.
{ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503, ECO:0000269|PubMed:7876189,
ECO:0000269|PubMed:8188594}.
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10515948,
ECO:0000269|PubMed:16279953}.
-!- PTM: Tryptophan tryptophylquinone (TTQ) is formed by oxidation of
the indole ring of a tryptophan to form tryptophylquinone followed
by covalent cross-linking with another tryptophan residue.
{ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503, ECO:0000269|PubMed:8188594}.
-!- PTM: Predicted to be exported by the Tat system. The position of
the signal peptide cleavage has been experimentally proven.
-!- SIMILARITY: Belongs to the aromatic amine dehydrogenase light
chain family. {ECO:0000305}.
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EMBL; AF302652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AM292629; CAL23525.1; -; Genomic_DNA.
RefSeq; WP_021447059.1; NZ_RHXK01000003.1.
PDB; 2AGL; X-ray; 1.40 A; D/H=48-182.
PDB; 2AGW; X-ray; 1.45 A; D/H=48-182.
PDB; 2AGX; X-ray; 2.20 A; D/H=48-182.
PDB; 2AGY; X-ray; 1.10 A; D/H=48-182.
PDB; 2AGZ; X-ray; 1.60 A; D/H=48-182.
PDB; 2AH0; X-ray; 1.45 A; D/H=48-182.
PDB; 2AH1; X-ray; 1.20 A; D/H=48-182.
PDB; 2H3X; X-ray; 2.50 A; B/E=48-182.
PDB; 2H47; X-ray; 2.60 A; B/E/G/I=48-182.
PDB; 2HJ4; X-ray; 1.80 A; D/H=48-182.
PDB; 2HJB; X-ray; 1.85 A; D/H=48-182.
PDB; 2HKM; X-ray; 1.50 A; D/H=48-182.
PDB; 2HKR; X-ray; 1.40 A; D/H=59-180.
PDB; 2HXC; X-ray; 1.45 A; D/H=48-182.
PDB; 2I0R; X-ray; 1.40 A; D/H=59-182.
PDB; 2I0S; X-ray; 1.40 A; D/H=59-182.
PDB; 2I0T; X-ray; 1.35 A; D/H=59-180.
PDB; 2IAA; X-ray; 1.95 A; B/E=48-182.
PDB; 2IUP; X-ray; 1.80 A; D/H=48-182.
PDB; 2IUQ; X-ray; 1.50 A; D/H=48-182.
PDB; 2IUR; X-ray; 1.30 A; D/H=48-182.
PDB; 2IUV; X-ray; 1.55 A; D/H=48-182.
PDB; 2OIZ; X-ray; 1.05 A; D/H=48-182.
PDB; 2OJY; X-ray; 1.60 A; D/H=48-180.
PDB; 2OK4; X-ray; 1.45 A; D/H=48-182.
PDB; 2OK6; X-ray; 1.45 A; D/H=48-182.
PDB; 2Q7Q; X-ray; 1.60 A; D/H=59-182.
PDBsum; 2AGL; -.
PDBsum; 2AGW; -.
PDBsum; 2AGX; -.
PDBsum; 2AGY; -.
PDBsum; 2AGZ; -.
PDBsum; 2AH0; -.
PDBsum; 2AH1; -.
PDBsum; 2H3X; -.
PDBsum; 2H47; -.
PDBsum; 2HJ4; -.
PDBsum; 2HJB; -.
PDBsum; 2HKM; -.
PDBsum; 2HKR; -.
PDBsum; 2HXC; -.
PDBsum; 2I0R; -.
PDBsum; 2I0S; -.
PDBsum; 2I0T; -.
PDBsum; 2IAA; -.
PDBsum; 2IUP; -.
PDBsum; 2IUQ; -.
PDBsum; 2IUR; -.
PDBsum; 2IUV; -.
PDBsum; 2OIZ; -.
PDBsum; 2OJY; -.
PDBsum; 2OK4; -.
PDBsum; 2OK6; -.
PDBsum; 2Q7Q; -.
SMR; P84887; -.
STRING; 511.JT27_04310; -.
DrugBank; DB08649; (1S)-1-AMINO-2-(1H-INDOL-3-YL)ETHANOL.
DrugBank; DB08652; 2-(1H-INDOL-3-YL)ACETAMIDE.
DrugBank; DB08653; 2-(1H-INDOL-3-YL)ETHANAMINE.
DrugBank; DB08767; 2-(4-METHOXYPHENYL)ACETAMIDE.
GeneID; 29369385; -.
KEGG; ag:CAL23525; -.
KO; K13371; -.
OrthoDB; 1619371at2; -.
BioCyc; MetaCyc:MONOMER-16554; -.
BRENDA; 1.4.9.2; 232.
SABIO-RK; P84887; -.
EvolutionaryTrace; P84887; -.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0030058; F:amine dehydrogenase activity; IEA:InterPro.
GO; GO:0030059; F:aralkylamine dehydrogenase (azurin) activity; IEA:UniProtKB-EC.
GO; GO:0009308; P:amine metabolic process; IEA:InterPro.
Gene3D; 2.60.30.10; -; 1.
InterPro; IPR016008; Amine_DH_Ltc.
InterPro; IPR036560; MADH/AADH_L_sf.
InterPro; IPR013504; MADH/AADH_Ltc_C_dom.
InterPro; IPR006311; TAT_signal.
Pfam; PF02975; Me-amine-dh_L; 1.
PIRSF; PIRSF000192; Amine_dh_beta; 1.
SUPFAM; SSF57561; SSF57561; 1.
PROSITE; PS51318; TAT; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Disulfide bond;
Electron transport; Oxidoreductase; Periplasm; Signal; Transport; TTQ.
SIGNAL 1 47 Tat-type signal. {ECO:0000255|PROSITE-
ProRule:PRU00648,
ECO:0000269|PubMed:16279953,
ECO:0000269|PubMed:8188594}.
CHAIN 48 182 Aralkylamine dehydrogenase light chain.
{ECO:0000255|PROSITE-ProRule:PRU00648,
ECO:0000269|PubMed:8188594}.
/FTId=PRO_0000287911.
REGION 156 158 Substrate-binding.
{ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560}.
ACT_SITE 109 109 Tryptophylquinone 6'-substrate hemiaminal
intermediate.
ACT_SITE 128 128 Proton acceptor.
{ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560}.
BINDING 84 84 Substrate. {ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560}.
SITE 172 172 Transition state stabilizer.
MOD_RES 109 109 Tryptophylquinone.
{ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503}.
DISULFID 75 140 {ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503}.
DISULFID 81 113 {ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503}.
DISULFID 88 171 {ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503}.
DISULFID 90 138 {ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503}.
DISULFID 91 135 {ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503}.
DISULFID 98 129 {ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503}.
DISULFID 130 161 {ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503}.
CROSSLNK 109 160 Tryptophan tryptophylquinone (Trp-Trp).
{ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503}.
HELIX 60 62 {ECO:0000244|PDB:2OIZ}.
HELIX 64 66 {ECO:0000244|PDB:2OIZ}.
HELIX 69 72 {ECO:0000244|PDB:2I0T}.
HELIX 78 80 {ECO:0000244|PDB:2OIZ}.
STRAND 84 87 {ECO:0000244|PDB:2OIZ}.
HELIX 88 90 {ECO:0000244|PDB:2OIZ}.
STRAND 95 97 {ECO:0000244|PDB:2IAA}.
STRAND 109 114 {ECO:0000244|PDB:2OIZ}.
TURN 116 118 {ECO:0000244|PDB:2OIZ}.
STRAND 121 126 {ECO:0000244|PDB:2OIZ}.
STRAND 128 132 {ECO:0000244|PDB:2OIZ}.
STRAND 137 141 {ECO:0000244|PDB:2OIZ}.
HELIX 149 154 {ECO:0000244|PDB:2OIZ}.
TURN 160 163 {ECO:0000244|PDB:2OIZ}.
STRAND 164 166 {ECO:0000244|PDB:2OIZ}.
STRAND 169 172 {ECO:0000244|PDB:2OIZ}.
STRAND 175 179 {ECO:0000244|PDB:2OIZ}.
SEQUENCE 182 AA; 19652 MW; 74BC95478B172A41 CRC64;
MRWLDKFGES LSRSVAHKTS RRSVLRSVGK LMVGSAFVLP VLPVARAAGG GGSSSGADHI
SLNPDLANED EVNSCDYWRH CAVDGFLCSC CGGTTTTCPP GSTPSPISWI GTCHNPHDGK
DYLISYHDCC GKTACGRCQC NTQTRERPGY EFFLHNDVNW CMANENSTFH CTTSVLVGLA
KN


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Related Genes :
[aauA] Aralkylamine dehydrogenase light chain (EC 1.4.9.2) (Aromatic amine dehydrogenase) (AADH)
[aauB] Aralkylamine dehydrogenase heavy chain (EC 1.4.9.2) (Aromatic amine dehydrogenase) (AADH)
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); 3C-like serine proteinase (3CLSP) (EC 3.4.21.-) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); 3C-like serine proteinase (3CLSP) (EC 3.4.21.-) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[qhnDH] Quinohemoprotein amine dehydrogenase subunit gamma (QH-AmDH) (EC 1.4.99.-) (Quinohemoprotein amine dehydrogenase 9 kDa subunit) (Quinohemoprotein amine dehydrogenase catalytic subunit)
[aro-1 aro-2 aro-4 aro-5 aro-9 B14H13.20 NCU016321] Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
[DHRS9 RDH15 SDR9C4 UNQ835/PRO1773] Dehydrogenase/reductase SDR family member 9 (EC 1.1.1.209) (EC 1.1.1.53) (3-alpha hydroxysteroid dehydrogenase) (3-alpha-HSD) (NADP-dependent retinol dehydrogenase/reductase) (RDH-E2) (RDHL) (Retinol dehydrogenase 15) (EC 1.1.1.105) (Short chain dehydrogenase/reductase family 9C member 4) (Short-chain dehydrogenase/reductase retSDR8) (Tracheobronchial epithelial cell-specific retinol dehydrogenase) (RDH-TBE)
[Aldh3a1 Ahd-4 Ahd4 Aldh3 Aldh4] Aldehyde dehydrogenase, dimeric NADP-preferring (EC 1.2.1.5) (Aldehyde dehydrogenase 4) (Aldehyde dehydrogenase family 3 member A1) (Dioxin-inducible aldehyde dehydrogenase 3)
[DHRS4 SDR25C2 UNQ851/PRO1800] Dehydrogenase/reductase SDR family member 4 (EC 1.1.1.184) (NADPH-dependent carbonyl reductase/NADP-retinol dehydrogenase) (CR) (PHCR) (NADPH-dependent retinol dehydrogenase/reductase) (NRDR) (humNRDR) (Peroxisomal short-chain alcohol dehydrogenase) (PSCD) (SCAD-SRL) (Short chain dehydrogenase/reductase family 25C member 2) (Short-chain dehydrogenase/reductase family member 4)
[Aldh9a1] 4-trimethylaminobutyraldehyde dehydrogenase (TMABA-DH) (TMABADH) (EC 1.2.1.47) (Aldehyde dehydrogenase family 9 member A1) (EC 1.2.1.3)
[RDH16 RODH4 SDR9C8] Retinol dehydrogenase 16 (EC 1.1.1.105) (EC 1.1.1.209) (EC 1.1.1.315) (EC 1.1.1.53) (Human epidermal retinol dehydrogenase) (hRDH-E) (Microsomal NAD(+)-dependent retinol dehydrogenase 4) (RoDH-4) (Short chain dehydrogenase/reductase family 9C member 8) (Sterol/retinol dehydrogenase)
[qhnDH] Quinohemoprotein amine dehydrogenase subunit gamma (QH-AmDH) (EC 1.4.99.-) (Quinohemoprotein amine dehydrogenase 9 kDa subunit) (Quinohemoprotein amine dehydrogenase catalytic subunit)
[AANAT SNAT] Serotonin N-acetyltransferase (Serotonin acetylase) (EC 2.3.1.87) (Aralkylamine N-acetyltransferase) (AA-NAT)
[ard-1 NCU00643] L-arabinitol 4-dehydrogenase (LAD) (EC 1.1.1.12)
[Dhrs4 D14Ucla2] Dehydrogenase/reductase SDR family member 4 (EC 1.1.1.184) (NADPH-dependent carbonyl reductase/NADP-retinol dehydrogenase) (CR) (PHCR) (NADPH-dependent retinol dehydrogenase/reductase) (NDRD) (mouNRDR) (Peroxisomal short-chain alcohol dehydrogenase) (PSCD)
[CAD4 CAD CAD-C CAD2 LCAD-C At3g19450 MLD14.19] Cinnamyl alcohol dehydrogenase 4 (AtCAD4) (EC 1.1.1.195) (Cinnamyl alcohol dehydrogenase C)
[RDH12 SDR7C2] Retinol dehydrogenase 12 (EC 1.1.1.300) (All-trans and 9-cis retinol dehydrogenase) (Short chain dehydrogenase/reductase family 7C member 2)
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BMT53_00170 BUE81_10670 BvCms12BK_01457 BvCms28BK_04168 BvCmsHHP001_02632 BvCmsKKP061_00566 BvCmsKSP008_02510 BvCmsKSP015_01352 BvCmsKSP036_04668 BvCmsKSP045_04450 BvCmsKSP058_03204 BvCmsKSP067_02879 BvCmsKSP083_03900 BvCmsNSNP027_04914 BvCmsNSP006_03750 BvCmsNSP007_03329 BvCmsNSP039_03266 BvCmsNSP047_03567 BvCmsNSP078_03451 BvCmsSINP011_04162 BvCmsSIP006_05510 BvCmsSIP082_02402 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 CDL37_00765 CIJ94_05515 COD46_23180 CQP61_17160 CRD98_26150 CY655_12940 D5618_21870 D9D20_21030 D9D43_06110 D9H68_20750 D9H70_25730 D9I87_15275 DL800_09215 DNQ41_14245 DQE83_22775 DTL43_21780 DTM25_06080 DU321_04440 E2855_02503 E2863_02392 EC95NR1_00961 ED648_25045 EFB45_10990 EPS97_16570 EPT01_11070 EQ825_23250 ERS085379_01273 ERS085386_05041 EVY21_22520 ExPECSC038_01920 EXX32_14605 EXX71_02385 EXX78_21815 EYD11_09165 HmCmsJML079_02678 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PU06_24500 SAMEA3472043_00447 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[F2] Prothrombin (EC 3.4.21.5) (Coagulation factor II) [Cleaved into: Activation peptide fragment 1; Activation peptide fragment 2; Thrombin light chain; Thrombin heavy chain]
[BCKDHA] 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial (EC 1.2.4.4) (Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain) (BCKDE1A) (BCKDH E1-alpha)
[CBR1 CBR CRN SDR21C1] Carbonyl reductase [NADPH] 1 (EC 1.1.1.184) (15-hydroxyprostaglandin dehydrogenase [NADP(+)]) (EC 1.1.1.197) (NADPH-dependent carbonyl reductase 1) (Prostaglandin 9-ketoreductase) (Prostaglandin-E(2) 9-reductase) (EC 1.1.1.189) (Short chain dehydrogenase/reductase family 21C member 1)
[RDH5 HSD17B9 RDH1 SDR9C5] Retinol dehydrogenase 5 (EC 1.1.1.209) (EC 1.1.1.315) (EC 1.1.1.53) (11-cis retinol dehydrogenase) (11-cis RDH) (11-cis RoDH) (9-cis retinol dehydrogenase) (9cRDH) (Short chain dehydrogenase/reductase family 9C member 5)
[hchA A8M42_01610 AM465_15370 AWF59_019055 AZZ83_004235 B9N33_26475 BFD68_20845 C1I57_21890 C7B02_06890 CCZ14_26645 CCZ17_22700 CRT43_11430 CT143_08220 D3C88_02905 D9D33_15385 D9E49_19020 D9I20_10460 D9J46_03345 DNR41_00375 DS966_16070 DU333_03260 DW236_02290 ECTO124_02024 EGT48_04930 EPS76_06485 EPS91_17475 EPS94_00505 ERS085406_02591 EWK56_00075 ExPECSC007_02422 ExPECSC065_02714 HmCmsJML122_02218 NCTC10766_03778 NCTC7928_05955 NCTC8450_02317 NCTC9007_02951 NCTC9075_02834 NCTC9775_01269 SY51_11150 U12A_02105 U14A_02105] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[hchA A9819_11910 ACN81_03425 AML35_08765 AW059_23935 BANRA_00208 BANRA_00433 BANRA_02614 BHF46_18455 BMT91_24760 BvCmsC61A_00149 BvCmsH15A_00510 BvCmsKSNP120_04693 BvCmsKSP026_03873 BvCmsKSP076_04891 C4J69_22715 C7B08_25495 CR538_10415 D2F89_25795 D3Y67_22910 D9G42_11130 D9I97_22010 D9J11_25195 DP258_02540 E5M00_18610 EC3234A_36c00010 EC382_21100 ECTO6_01955 EFV06_13085 EPS71_23885 FORC82_1921 NCTC8500_02249 NCTC9037_02122 NCTC9117_02637 NCTC9969_02156 SAMEA3472108_01151 SAMEA3484427_04795 SAMEA3484429_02051 SAMEA3752557_05476 SAMEA3752559_04333] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[ADH4] All-trans-retinol dehydrogenase [NAD(+)] ADH4 (EC 1.1.1.105) (Alcohol dehydrogenase 4) (Alcohol dehydrogenase class II pi chain)
[HSD11B2 HSD11K SDR9C3] Corticosteroid 11-beta-dehydrogenase isozyme 2 (EC 1.1.1.-) (11-beta-hydroxysteroid dehydrogenase type 2) (11-DH2) (11-beta-HSD2) (11-beta-hydroxysteroid dehydrogenase type II) (11-HSD type II) (11-beta-HSD type II) (NAD-dependent 11-beta-hydroxysteroid dehydrogenase) (11-beta-HSD) (Short chain dehydrogenase/reductase family 9C member 3)
[BCKDHB] 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial (EC 1.2.4.4) (Branched-chain alpha-keto acid dehydrogenase E1 component beta chain) (BCKDE1B) (BCKDH E1-beta)
[K503DRAFT_817084] Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
[kgd sucA MSMEG_5049 MSMEI_4922] Multifunctional 2-oxoglutarate metabolism enzyme (2-hydroxy-3-oxoadipate synthase) (HOA synthase) (HOAS) (EC 2.2.1.5) (2-oxoglutarate carboxy-lyase) (2-oxoglutarate decarboxylase) (Alpha-ketoglutarate decarboxylase) (KG decarboxylase) (KGD) (EC 4.1.1.71) (Alpha-ketoglutarate-glyoxylate carboligase) [Includes: 2-oxoglutarate dehydrogenase E1 component (ODH E1 component) (EC 1.2.4.2) (Alpha-ketoglutarate dehydrogenase E1 component) (KDH E1 component); Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (EC 2.3.1.61) (2-oxoglutarate dehydrogenase complex E2 component) (ODH E2 component) (OGDC-E2) (Dihydrolipoamide succinyltransferase)]
[HSD17B10 ERAB HADH2 MRPP2 SCHAD SDR5C1 XH98G2] 3-hydroxyacyl-CoA dehydrogenase type-2 (EC 1.1.1.35) (17-beta-hydroxysteroid dehydrogenase 10) (17-beta-HSD 10) (EC 1.1.1.51) (2-methyl-3-hydroxybutyryl-CoA dehydrogenase) (MHBD) (3-hydroxy-2-methylbutyryl-CoA dehydrogenase) (EC 1.1.1.178) (3-hydroxyacyl-CoA dehydrogenase type II) (Endoplasmic reticulum-associated amyloid beta-peptide-binding protein) (Mitochondrial ribonuclease P protein 2) (Mitochondrial RNase P protein 2) (Short chain dehydrogenase/reductase family 5C member 1) (Short-chain type dehydrogenase/reductase XH98G2) (Type II HADH)

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