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Q8TDX5 (ACMSD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2-amino-3-carboxymuconate-6-semialdehyde decarboxylase

EC=4.1.1.45
Alternative name(s):
Picolinate carboxylase
Gene names
Name:ACMSD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length336 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.5

Catalytic activity

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

Pathway

Secondary metabolite metabolism; quinolate metabolism.

Subunit structure

Monomer. Ref.5

Sequence similarities

Belongs to the ACMSD family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 (identifier: Q8TDX5-1)

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.
Isoform 2 (identifier: Q8TDX5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: Missing.
     59-83: RIREMDQKGVTVQALSTVPVMFSYW → MGKSSEWCERIAGIQKFVLEKWTKK
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3363362-amino-3-carboxymuconate-6-semialdehyde decarboxylase
PRO_0000190979

Sites

Metal binding61Zinc
Metal binding81Zinc
Metal binding1741Zinc
Metal binding2911Zinc
Binding site471Substrate Probable

Natural variations

Alternative sequence1 – 5858Missing in isoform 2.
VSP_050622
Alternative sequence59 – 8325RIREM…MFSYW → MGKSSEWCERIAGIQKFVLE KWTKK in isoform 2.
VSP_050623

Secondary structure

.............................................................. 336
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 892B01D2A77C35A5

FASTA33638,035
        10         20         30         40         50         60 
MKIDIHSHIL PKEWPDLKKR FGYGGWVQLQ HHSKGEAKLL KDGKVFRVVR ENCWDPEVRI 

        70         80         90        100        110        120 
REMDQKGVTV QALSTVPVMF SYWAKPEDTL NLCQLLNNDL ASTVVSYPRR FVGLGTLPMQ 

       130        140        150        160        170        180 
APELAVKEME RCVKELGFPG VQIGTHVNEW DLNAQELFPV YAAAERLKCS LFVHPWDMQM 

       190        200        210        220        230        240 
DGRMAKYWLP WLVGMPAETT IAICSMIMGG VFEKFPKLKV CFAHGGGAFP FTVGRISHGF 

       250        260        270        280        290        300 
SMRPDLCAQD NPMNPKKYLG SFYTDALVHD PLSLKLLTDV IGKDKVILGT DYPFPLGELE 

       310        320        330 
PGKLIESMEE FDEETKNKLK AGNALAFLGL ERKQFE 

« Hide

Isoform 2 [UniParc].

Checksum: 4F7B961D6B0C9185
Show »

FASTA27831,213

References

« Hide 'large scale' references
[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: Brain.
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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 Liver.
[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 DHAP, FUNCTION, SUBUNIT, ZINC-BINDING SITES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2173.2. [Q8TDX5-1]
RefSeqNP_612199.2. NM_138326.2. [Q8TDX5-1]
XP_005263644.1. XM_005263587.2. [Q8TDX5-2]
XP_005263645.1. XM_005263588.2. [Q8TDX5-2]
UniGeneHs.655728.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ8TDX5.
SMRQ8TDX5. Positions 1-332.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid126217. 1 interaction.
IntActQ8TDX5. 1 interaction.
MINTMINT-1479806.
STRING9606.ENSP00000348459.

PTM databases

PhosphoSiteQ8TDX5.

Proteomic databases

PaxDbQ8TDX5.
PRIDEQ8TDX5.

Protocols and materials databases

DNASU130013.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000283054; ENSP00000283054; ENSG00000153086. [Q8TDX5-2]
ENST00000356140; ENSP00000348459; ENSG00000153086. [Q8TDX5-1]
ENST00000392928; ENSP00000376659; ENSG00000153086. [Q8TDX5-2]
GeneID130013.
KEGGhsa:130013.
UCSCuc002ttz.3. human. [Q8TDX5-1]
uc002tua.3. human. [Q8TDX5-2]

Organism-specific databases

CTD130013.
GeneCardsGC02P135596.
H-InvDBHIX0019780.
HGNCHGNC:19288. ACMSD.
HPAHPA010533.
HPA011179.
MIM608889. gene.
neXtProtNX_Q8TDX5.
PharmGKBPA134973312.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2159.
HOGENOMHOG000254105.
HOVERGENHBG050450.
InParanoidQ8TDX5.
KOK03392.
OMAGFNMRPD.
OrthoDBEOG7WDN2Q.
PhylomeDBQ8TDX5.
TreeFamTF313232.

Enzyme and pathway databases

BioCycMetaCyc:HS14455-MONOMER.
BRENDA4.1.1.45. 2681.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00270.

Gene expression databases

BgeeQ8TDX5.
CleanExHS_ACMSD.
GenevestigatorQ8TDX5.

Family and domain databases

InterProIPR006992. Amidohydro_2.
[Graphical view]
PfamPF04909. Amidohydro_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8TDX5.
GenomeRNAi130013.
NextBio82680.
PROQ8TDX5.
SOURCESearch...

Entry information

Entry nameACMSD_HUMAN
AccessionPrimary (citable) accession number: Q8TDX5
Secondary accession number(s): Q3B7X3, Q53SR5, Q96KY2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: June 1, 2002
Last modified: July 9, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM