AMNC_PSESP
ID AMNC_PSESP Reviewed; 491 AA.
AC Q9KWS5;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=2-aminomuconic 6-semialdehyde dehydrogenase;
DE EC=1.2.1.32;
DE AltName: Full=Aminomuconate-semialdehyde dehydrogenase;
GN Name=amnC;
OS Pseudomonas sp.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=306;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=AP-3;
RX PubMed=9169437; DOI=10.1074/jbc.272.23.14727;
RA Takenaka S., Murakami S., Shinke R., Hatakeyama K., Yukawa H., Aoki K.;
RT "Novel genes encoding 2-aminophenol 1,6-dioxygenase from Pseudomonas
RT species AP-3 growing on 2-aminophenol and catalytic properties of the
RT purified enzyme.";
RL J. Biol. Chem. 272:14727-14732(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBSTRATE SPECIFICITY,
RP AND ACTIVITY REGULATION.
RC STRAIN=AP-3;
RX PubMed=11081795; DOI=10.1007/s002030000203;
RA Takenaka S., Murakami S., Kim Y.J., Aoki K.;
RT "Complete nucleotide sequence and functional analysis of the genes for 2-
RT aminophenol metabolism from Pseudomonas sp. AP-3.";
RL Arch. Microbiol. 174:265-272(2000).
CC -!- FUNCTION: Involved in the modified meta-cleavage pathway for 2-
CC aminophenol catabolism. The enzyme is also active toward 2-
CC hydroxymuconic 6-semialdehyde, acetaldehyde, propionaldehyde, and
CC butyraldehyde. {ECO:0000269|PubMed:9169437}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-aminomuconate 6-semialdehyde + H2O + NAD(+) = (2Z,4E)-2-
CC aminomuconate + 2 H(+) + NADH; Xref=Rhea:RHEA:14469,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:77634, ChEBI:CHEBI:77859; EC=1.2.1.32;
CC Evidence={ECO:0000269|PubMed:11081795};
CC -!- ACTIVITY REGULATION: Strongly inhibited by Ag(+) and Hg(+), and
CC comnpletely inhibited by p-chloromercuribenzoic acid.
CC {ECO:0000269|PubMed:11081795}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. Stable in the range of pH 6.0-8.0.
CC {ECO:0000269|PubMed:11081795};
CC Temperature dependence:
CC After heating at 40 degrees Celsius, the remaining activity is 40% of
CC the original activity. {ECO:0000269|PubMed:11081795};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:11081795}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AB020521; BAB03533.1; -; Genomic_DNA.
DR PDB; 7BZV; X-ray; 1.99 A; A/B=1-491.
DR PDBsum; 7BZV; -.
DR AlphaFoldDB; Q9KWS5; -.
DR SMR; Q9KWS5; -.
DR BioCyc; MetaCyc:MON-14741; -.
DR GO; GO:0047102; F:aminomuconate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 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 InterPro; IPR017628; OHmuconic_semiald_DH.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR03216; OH_muco_semi_DH; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Direct protein sequencing;
KW NAD; Oxidoreductase.
FT CHAIN 1..491
FT /note="2-aminomuconic 6-semialdehyde dehydrogenase"
FT /id="PRO_0000383023"
FT ACT_SITE 252
FT /evidence="ECO:0000250"
FT ACT_SITE 286
FT /evidence="ECO:0000250"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:7BZV"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:7BZV"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:7BZV"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:7BZV"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:7BZV"
FT HELIX 38..52
FT /evidence="ECO:0007829|PDB:7BZV"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:7BZV"
FT HELIX 61..77
FT /evidence="ECO:0007829|PDB:7BZV"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:7BZV"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:7BZV"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:7BZV"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:7BZV"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:7BZV"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:7BZV"
FT STRAND 133..142
FT /evidence="ECO:0007829|PDB:7BZV"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:7BZV"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:7BZV"
FT HELIX 155..168
FT /evidence="ECO:0007829|PDB:7BZV"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:7BZV"
FT HELIX 183..195
FT /evidence="ECO:0007829|PDB:7BZV"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:7BZV"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:7BZV"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:7BZV"
FT HELIX 232..243
FT /evidence="ECO:0007829|PDB:7BZV"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:7BZV"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:7BZV"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:7BZV"
FT HELIX 267..279
FT /evidence="ECO:0007829|PDB:7BZV"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:7BZV"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:7BZV"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:7BZV"
FT HELIX 299..311
FT /evidence="ECO:0007829|PDB:7BZV"
FT HELIX 331..346
FT /evidence="ECO:0007829|PDB:7BZV"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:7BZV"
FT HELIX 363..366
FT /evidence="ECO:0007829|PDB:7BZV"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:7BZV"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:7BZV"
FT STRAND 391..399
FT /evidence="ECO:0007829|PDB:7BZV"
FT HELIX 402..410
FT /evidence="ECO:0007829|PDB:7BZV"
FT STRAND 416..421
FT /evidence="ECO:0007829|PDB:7BZV"
FT HELIX 425..434
FT /evidence="ECO:0007829|PDB:7BZV"
FT STRAND 437..443
FT /evidence="ECO:0007829|PDB:7BZV"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:7BZV"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:7BZV"
FT HELIX 467..473
FT /evidence="ECO:0007829|PDB:7BZV"
FT STRAND 475..484
FT /evidence="ECO:0007829|PDB:7BZV"
SQ SEQUENCE 491 AA; 53722 MW; 1B196D37FF534551 CRC64;
MKQYRNFVDG KWVESSKTFQ DVTPIDGSVV AVVHEADRDL VDAAVKAGHR ALEGEWGRTT
AAQRVDWLRR IANEMERRQQ DFLDAEMADT GKPLSMAATI DIPRGIANFR NFADILATAP
VDSHRLDLPD GAYALNYAAR KPLGVVGVIS PWNLPLLLLT WKVAPALACG NAVVVKPSED
TPGTATLLAE VMEAVGIPPG VFNLVHGFGP NSAGEFISQH PDISAITFTG ESKTGSTIMR
AAAEGVKPVS FELGGKNAAV IFADCDFEKM LDGMMRALFL NSGQVCLCSE RVYVERPIFD
RFCVALAERI KALKVDWPHE TDTQMGPLIS SKHRDKVLSY FELARQEGAT FLAGGGVPRF
GDERDNGAWV EPTVIAGLSD DARVVREEIF GPICHVTPFD SESEVIRRAN DTRYGLAATI
WTTNLSRAHR VSELMRVGIS WVNTWFLRDL RTPFGGAGLS GIGREGGMHS LNFYSELTNV
CVRIDKESPD V
