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Q8TDX5

- ACMSD_HUMAN

UniProt

Q8TDX5 - ACMSD_HUMAN

Protein

2-amino-3-carboxymuconate-6-semialdehyde decarboxylase

Gene

ACMSD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    Functioni

    Converts alpha-amino-beta-carboxymuconate-epsilon-semialdehyde (ACMS) to alpha-aminomuconate semialdehyde (AMS). ACMS can be converted non-enzymatically to quinolate (QA), a key precursor of NAD, and a potent endogenous excitotoxin of neuronal cells which is implicated in the pathogenesis of various neurodegenerative disorders. In the presence of ACMSD, ACMS is converted to AMS, a benign catabolite. ACMSD ultimately controls the metabolic fate of tryptophan catabolism along the kynurenine pathway.1 Publication

    Catalytic activityi

    2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate = 2-aminomuconate semialdehyde + CO2.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi6 – 61Zinc
    Metal bindingi8 – 81Zinc
    Binding sitei47 – 471SubstrateCurated
    Metal bindingi174 – 1741Zinc
    Metal bindingi291 – 2911Zinc

    GO - Molecular functioni

    1. aminocarboxymuconate-semialdehyde decarboxylase activity Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. cellular nitrogen compound metabolic process Source: Reactome
    2. quinolinate metabolic process Source: UniProtKB
    3. small molecule metabolic process Source: Reactome
    4. tryptophan catabolic process Source: Reactome

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:HS14455-MONOMER.
    BRENDAi4.1.1.45. 2681.
    ReactomeiREACT_916. Tryptophan catabolism.
    UniPathwayiUPA00270.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-amino-3-carboxymuconate-6-semialdehyde decarboxylase (EC:4.1.1.45)
    Alternative name(s):
    Picolinate carboxylase
    Gene namesi
    Name:ACMSD
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:19288. ACMSD.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134973312.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3363362-amino-3-carboxymuconate-6-semialdehyde decarboxylasePRO_0000190979Add
    BLAST

    Proteomic databases

    PaxDbiQ8TDX5.
    PRIDEiQ8TDX5.

    PTM databases

    PhosphoSiteiQ8TDX5.

    Expressioni

    Gene expression databases

    BgeeiQ8TDX5.
    CleanExiHS_ACMSD.
    GenevestigatoriQ8TDX5.

    Organism-specific databases

    HPAiHPA010533.
    HPA011179.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi126217. 1 interaction.
    IntActiQ8TDX5. 1 interaction.
    MINTiMINT-1479806.
    STRINGi9606.ENSP00000348459.

    Structurei

    Secondary structure

    1
    336
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86
    Helixi17 – 215
    Beta strandi27 – 337
    Beta strandi36 – 416
    Beta strandi44 – 507
    Helixi51 – 533
    Helixi56 – 6611
    Beta strandi70 – 745
    Helixi77 – 804
    Helixi86 – 10621
    Turni108 – 1103
    Beta strandi111 – 1155
    Helixi122 – 13413
    Beta strandi139 – 1479
    Helixi155 – 1573
    Helixi158 – 16710
    Beta strandi170 – 1745
    Helixi182 – 1843
    Helixi189 – 1924
    Helixi194 – 20815
    Helixi211 – 2144
    Beta strandi220 – 2234
    Helixi224 – 2263
    Helixi229 – 24214
    Helixi244 – 2474
    Beta strandi248 – 2503
    Helixi255 – 2584
    Beta strandi261 – 2655
    Helixi271 – 28111
    Beta strandi285 – 2873
    Helixi303 – 3064
    Helixi313 – 3208
    Helixi322 – 3287

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WM1X-ray2.01A1-336[»]
    4IGMX-ray2.39A/B/C/D/E/F1-332[»]
    4IGNX-ray2.33A/B/C/D/E/F1-332[»]
    4IH3X-ray2.49A/B/C/D/E/F1-332[»]
    ProteinModelPortaliQ8TDX5.
    SMRiQ8TDX5. Positions 1-332.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8TDX5.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ACMSD family.Curated

    Phylogenomic databases

    eggNOGiCOG2159.
    HOGENOMiHOG000254105.
    HOVERGENiHBG050450.
    InParanoidiQ8TDX5.
    KOiK03392.
    OMAiGFNMRPD.
    OrthoDBiEOG7WDN2Q.
    PhylomeDBiQ8TDX5.
    TreeFamiTF313232.

    Family and domain databases

    InterProiIPR006992. Amidohydro_2.
    [Graphical view]
    PfamiPF04909. Amidohydro_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q8TDX5-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MKIDIHSHIL PKEWPDLKKR FGYGGWVQLQ HHSKGEAKLL KDGKVFRVVR    50
    ENCWDPEVRI REMDQKGVTV QALSTVPVMF SYWAKPEDTL NLCQLLNNDL 100
    ASTVVSYPRR FVGLGTLPMQ APELAVKEME RCVKELGFPG VQIGTHVNEW 150
    DLNAQELFPV YAAAERLKCS LFVHPWDMQM DGRMAKYWLP WLVGMPAETT 200
    IAICSMIMGG VFEKFPKLKV CFAHGGGAFP FTVGRISHGF SMRPDLCAQD 250
    NPMNPKKYLG SFYTDALVHD PLSLKLLTDV IGKDKVILGT DYPFPLGELE 300
    PGKLIESMEE FDEETKNKLK AGNALAFLGL ERKQFE 336
    Length:336
    Mass (Da):38,035
    Last modified:June 1, 2002 - v1
    Checksum:i892B01D2A77C35A5
    GO
    Isoform 2Curated (identifier: Q8TDX5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-58: Missing.
         59-83: RIREMDQKGVTVQALSTVPVMFSYW → MGKSSEWCERIAGIQKFVLEKWTKK

    Note: No experimental confirmation available.Curated

    Show »
    Length:278
    Mass (Da):31,213
    Checksum:i4F7B961D6B0C9185
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5858Missing in isoform 2. 1 PublicationVSP_050622Add
    BLAST
    Alternative sequencei59 – 8325RIREM…MFSYW → MGKSSEWCERIAGIQKFVLE KWTKK in isoform 2. 1 PublicationVSP_050623Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB071418 mRNA. Translation: BAB86938.1.
    AC016725 Genomic DNA. Translation: AAY14997.1.
    CH471058 Genomic DNA. Translation: EAX11650.1.
    CH471058 Genomic DNA. Translation: EAX11651.1.
    CH471058 Genomic DNA. Translation: EAX11652.1.
    BC016018 mRNA. Translation: AAH16018.1.
    BC107420 mRNA. Translation: AAI07421.1.
    CCDSiCCDS2173.2. [Q8TDX5-1]
    RefSeqiNP_612199.2. NM_138326.2. [Q8TDX5-1]
    XP_005263644.1. XM_005263587.2. [Q8TDX5-2]
    XP_005263645.1. XM_005263588.2. [Q8TDX5-2]
    UniGeneiHs.655728.

    Genome annotation databases

    EnsembliENST00000356140; ENSP00000348459; ENSG00000153086. [Q8TDX5-1]
    ENST00000392928; ENSP00000376659; ENSG00000153086. [Q8TDX5-2]
    GeneIDi130013.
    KEGGihsa:130013.
    UCSCiuc002ttz.3. human. [Q8TDX5-1]
    uc002tua.3. human. [Q8TDX5-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB071418 mRNA. Translation: BAB86938.1 .
    AC016725 Genomic DNA. Translation: AAY14997.1 .
    CH471058 Genomic DNA. Translation: EAX11650.1 .
    CH471058 Genomic DNA. Translation: EAX11651.1 .
    CH471058 Genomic DNA. Translation: EAX11652.1 .
    BC016018 mRNA. Translation: AAH16018.1 .
    BC107420 mRNA. Translation: AAI07421.1 .
    CCDSi CCDS2173.2. [Q8TDX5-1 ]
    RefSeqi NP_612199.2. NM_138326.2. [Q8TDX5-1 ]
    XP_005263644.1. XM_005263587.2. [Q8TDX5-2 ]
    XP_005263645.1. XM_005263588.2. [Q8TDX5-2 ]
    UniGenei Hs.655728.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WM1 X-ray 2.01 A 1-336 [» ]
    4IGM X-ray 2.39 A/B/C/D/E/F 1-332 [» ]
    4IGN X-ray 2.33 A/B/C/D/E/F 1-332 [» ]
    4IH3 X-ray 2.49 A/B/C/D/E/F 1-332 [» ]
    ProteinModelPortali Q8TDX5.
    SMRi Q8TDX5. Positions 1-332.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 126217. 1 interaction.
    IntActi Q8TDX5. 1 interaction.
    MINTi MINT-1479806.
    STRINGi 9606.ENSP00000348459.

    PTM databases

    PhosphoSitei Q8TDX5.

    Proteomic databases

    PaxDbi Q8TDX5.
    PRIDEi Q8TDX5.

    Protocols and materials databases

    DNASUi 130013.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356140 ; ENSP00000348459 ; ENSG00000153086 . [Q8TDX5-1 ]
    ENST00000392928 ; ENSP00000376659 ; ENSG00000153086 . [Q8TDX5-2 ]
    GeneIDi 130013.
    KEGGi hsa:130013.
    UCSCi uc002ttz.3. human. [Q8TDX5-1 ]
    uc002tua.3. human. [Q8TDX5-2 ]

    Organism-specific databases

    CTDi 130013.
    GeneCardsi GC02P135596.
    H-InvDB HIX0019780.
    HGNCi HGNC:19288. ACMSD.
    HPAi HPA010533.
    HPA011179.
    MIMi 608889. gene.
    neXtProti NX_Q8TDX5.
    PharmGKBi PA134973312.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2159.
    HOGENOMi HOG000254105.
    HOVERGENi HBG050450.
    InParanoidi Q8TDX5.
    KOi K03392.
    OMAi GFNMRPD.
    OrthoDBi EOG7WDN2Q.
    PhylomeDBi Q8TDX5.
    TreeFami TF313232.

    Enzyme and pathway databases

    UniPathwayi UPA00270 .
    BioCyci MetaCyc:HS14455-MONOMER.
    BRENDAi 4.1.1.45. 2681.
    Reactomei REACT_916. Tryptophan catabolism.

    Miscellaneous databases

    EvolutionaryTracei Q8TDX5.
    GenomeRNAii 130013.
    NextBioi 82680.
    PROi Q8TDX5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8TDX5.
    CleanExi HS_ACMSD.
    Genevestigatori Q8TDX5.

    Family and domain databases

    InterProi IPR006992. Amidohydro_2.
    [Graphical view ]
    Pfami PF04909. Amidohydro_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and expression of a cDNA encoding human alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase (ACMSD). A key enzyme for the tryptophan-niacine pathway and 'quinolinate hypothesis'."
      Fukuoka S., Ishiguro K., Yanagihara K., Tanabe A., Egashira Y., Sanada H., Shibata K.
      J. Biol. Chem. 277:35162-35167(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY.
      Tissue: Brain1 Publication.
    2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Kidney and LiverImported.
    5. "The crystal structure of human alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase in complex with 1,3-dihydroxyacetonephosphate suggests a regulatory link between NAD synthesis and glycolysis."
      Garavaglia S., Perozzi S., Galeazzi L., Raffaelli N., Rizzi M.
      FEBS J. 276:6615-6623(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND DHAP, FUNCTION, SUBUNIT, ZINC-BINDING SITES.

    Entry informationi

    Entry nameiACMSD_HUMAN
    AccessioniPrimary (citable) accession number: Q8TDX5
    Secondary accession number(s): Q3B7X3, Q53SR5, Q96KY2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 24, 2003
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 103 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3