ACMSD_DICDI
ID ACMSD_DICDI Reviewed; 359 AA.
AC Q54LN9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=2-amino-3-carboxymuconate-6-semialdehyde decarboxylase;
DE EC=4.1.1.45;
DE AltName: Full=Picolinate carboxylase;
GN Name=acmsd; ORFNames=DDB_G0286525;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Converts alpha-amino-beta-carboxymuconate-epsilon-
CC semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-amino-3-carboxymuconate 6-semialdehyde + H(+) = 2-
CC aminomuconate 6-semialdehyde + CO2; Xref=Rhea:RHEA:16557,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:77634,
CC ChEBI:CHEBI:77803; EC=4.1.1.45;
CC -!- PATHWAY: Secondary metabolite metabolism; quinolate metabolism.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC ACMSD family. {ECO:0000305}.
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DR EMBL; AAFI02000087; EAL64189.1; -; Genomic_DNA.
DR RefSeq; XP_637693.1; XM_632601.1.
DR AlphaFoldDB; Q54LN9; -.
DR SMR; Q54LN9; -.
DR STRING; 44689.DDB0266468; -.
DR PaxDb; Q54LN9; -.
DR EnsemblProtists; EAL64189; EAL64189; DDB_G0286525.
DR GeneID; 8625659; -.
DR KEGG; ddi:DDB_G0286525; -.
DR dictyBase; DDB_G0286525; acmsd.
DR eggNOG; KOG4245; Eukaryota.
DR HOGENOM; CLU_039329_1_2_1; -.
DR InParanoid; Q54LN9; -.
DR OMA; TTNYKAI; -.
DR PhylomeDB; Q54LN9; -.
DR UniPathway; UPA00270; -.
DR PRO; PR:Q54LN9; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0001760; F:aminocarboxymuconate-semialdehyde decarboxylase activity; ISS:UniProtKB.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1904985; P:negative regulation of quinolinate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0019748; P:secondary metabolic process; IBA:GO_Central.
DR InterPro; IPR032465; ACMSD.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR21240; PTHR21240; 1.
DR Pfam; PF04909; Amidohydro_2; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..359
FT /note="2-amino-3-carboxymuconate-6-semialdehyde
FT decarboxylase"
FT /id="PRO_0000327893"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 359 AA; 40451 MW; 50DDD1BDEE180594 CRC64;
MENKETTTTT TTTNNGSDKK KRSLKIDLHT HILPKNWPNL KEKYGYGGWV SLDHHCSCKA
KMMIDGKFFR EIDSNCWDPD VRIQELNRDD VDIQVLSTVP VMFGYWAKPQ DALDLAQYLN
DHIAQVVSEN PKRFIGLGSL PMQCTESSIQ ELRRCILELG LPGIQIGSNV NGKNLDDPSL
FPIFEECEKL GAAVFIHPWE MVGKDRMPQY WLPWLVGMPA ETCLAICSMI FGGVFQRLPN
LKVCFAHGGG SFPFTIGRIE HGFNARPDLC AVVNPINPRE YIGKFWVDSL VHDEEALKFL
VNLMGEKKVT LGTDYPFPLG ELVPGQLIES IKEFSETTKE NLLGGNALEF LGLDPNKYL
