ACMSD_MOUSE
ID ACMSD_MOUSE Reviewed; 336 AA.
AC Q8R519; B9EI97; Q3UNW3;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=2-amino-3-carboxymuconate-6-semialdehyde decarboxylase;
DE EC=4.1.1.45;
DE AltName: Full=Picolinate carboxylase;
GN Name=Acmsd;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:BAB86939.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
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:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-194, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12140278; DOI=10.1074/jbc.m200819200;
RA Fukuoka S., Ishiguro K., Yanagihara K., Tanabe A., Egashira Y., Sanada H.,
RA Shibata K.;
RT "Identification and expression of a cDNA encoding human alpha-amino-beta-
RT carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD). A key enzyme
RT for the tryptophan-niacine pathway and 'quinolinate hypothesis'.";
RL J. Biol. Chem. 277:35162-35167(2002).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Converts alpha-amino-beta-carboxymuconate-epsilon-
CC semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS). ACMS can
CC be converted non-enzymatically to quinolate (QA), a key precursor of
CC NAD, and a potent endogenous excitotoxin of neuronal cells which is
CC implicated in the pathogenesis of various neurodegenerative disorders.
CC In the presence of ACMSD, ACMS is converted to AMS, a benign
CC catabolite. ACMSD ultimately controls the metabolic fate of tryptophan
CC catabolism along the kynurenine pathway.
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 -!- TISSUE SPECIFICITY: Highest expression in kidney with lower levels in
CC liver and brain. {ECO:0000269|PubMed:12140278}.
CC -!- INDUCTION: By streptozocin-induced diabetes. Repressed by low protein
CC diet. {ECO:0000269|PubMed:12140278}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC ACMSD family. {ECO:0000305}.
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DR EMBL; AK143962; BAE25634.1; -; mRNA.
DR EMBL; BC139281; AAI39282.1; -; mRNA.
DR EMBL; AB071419; BAB86939.1; -; mRNA.
DR CCDS; CCDS15247.1; -.
DR RefSeq; NP_001028213.1; NM_001033041.2.
DR AlphaFoldDB; Q8R519; -.
DR SMR; Q8R519; -.
DR BioGRID; 234466; 1.
DR STRING; 10090.ENSMUSP00000048482; -.
DR ChEMBL; CHEMBL4523405; -.
DR iPTMnet; Q8R519; -.
DR PhosphoSitePlus; Q8R519; -.
DR jPOST; Q8R519; -.
DR MaxQB; Q8R519; -.
DR PaxDb; Q8R519; -.
DR PRIDE; Q8R519; -.
DR ProteomicsDB; 285588; -.
DR Antibodypedia; 2546; 119 antibodies from 20 providers.
DR DNASU; 266645; -.
DR Ensembl; ENSMUST00000038006; ENSMUSP00000048482; ENSMUSG00000026348.
DR GeneID; 266645; -.
DR KEGG; mmu:266645; -.
DR UCSC; uc007ckv.1; mouse.
DR CTD; 130013; -.
DR MGI; MGI:2386323; Acmsd.
DR VEuPathDB; HostDB:ENSMUSG00000026348; -.
DR eggNOG; KOG4245; Eukaryota.
DR GeneTree; ENSGT00490000043417; -.
DR HOGENOM; CLU_039329_1_2_1; -.
DR InParanoid; Q8R519; -.
DR OMA; TTNYKAI; -.
DR OrthoDB; 941496at2759; -.
DR PhylomeDB; Q8R519; -.
DR TreeFam; TF313232; -.
DR BRENDA; 4.1.1.45; 3474.
DR UniPathway; UPA00270; -.
DR BioGRID-ORCS; 266645; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Acmsd; mouse.
DR PRO; PR:Q8R519; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8R519; protein.
DR Bgee; ENSMUSG00000026348; Expressed in right kidney and 20 other tissues.
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:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0007568; P:aging; ISO:MGI.
DR GO; GO:1904985; P:negative regulation of quinolinate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0046874; P:quinolinate metabolic process; ISO:MGI.
DR GO; GO:0019748; P:secondary metabolic process; IBA:GO_Central.
DR GO; GO:0006569; P:tryptophan catabolic process; ISO:MGI.
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 1: Evidence at protein level;
KW Decarboxylase; Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..336
FT /note="2-amino-3-carboxymuconate-6-semialdehyde
FT decarboxylase"
FT /id="PRO_0000190980"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 336 AA; 38027 MW; B01104827D161A9A CRC64;
MKIDIHTHIL PKEWPDLEKR FGYGGWVQLQ QQGKGEAKMI KDGKLFRVIQ QNCWDPEVRI
REMNQKGVTV QALSTVPVMF SYWAKPKDTL ELCQFLNNDL AATVARYPRR FVGLGTLPMQ
APELAVEEME RCVKALGFPG IQIGSHINTW DLNDPELFPI YAAAERLNCS LFVHPWDMQM
DGRMAKYWLP WLVGMPSETT MAICSMIMGG VFEKFPKLKV CFAHGGGAFP FTIGRIAHGF
NMRPDLCAQD NPSDPRKYLG SFYTDSLVHD PLSLKLLTDV IGKDKVMLGT DYPFPLGEQE
PGKLIESMAE FDEETKDKLT AGNALAFLGL ERKLFE
