MTND_HUMAN
ID MTND_HUMAN Reviewed; 179 AA.
AC Q9BV57; D6W4Y3; Q53HW3; Q53QD3; Q57YV7; Q68CK2; Q6ZSF7; Q7Z512; Q96P85;
AC Q9NV57;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Acireductone dioxygenase {ECO:0000255|HAMAP-Rule:MF_03154};
DE AltName: Full=Acireductone dioxygenase (Fe(2+)-requiring) {ECO:0000255|HAMAP-Rule:MF_03154};
DE Short=ARD' {ECO:0000255|HAMAP-Rule:MF_03154};
DE Short=Fe-ARD {ECO:0000255|HAMAP-Rule:MF_03154};
DE EC=1.13.11.54 {ECO:0000269|PubMed:15938715};
DE AltName: Full=Acireductone dioxygenase (Ni(2+)-requiring) {ECO:0000255|HAMAP-Rule:MF_03154};
DE Short=ARD {ECO:0000255|HAMAP-Rule:MF_03154};
DE Short=Ni-ARD {ECO:0000255|HAMAP-Rule:MF_03154};
DE EC=1.13.11.53 {ECO:0000255|HAMAP-Rule:MF_03154};
DE AltName: Full=Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1 {ECO:0000255|HAMAP-Rule:MF_03154};
DE Short=MTCBP-1 {ECO:0000255|HAMAP-Rule:MF_03154};
DE AltName: Full=Submergence-induced protein-like factor {ECO:0000303|Ref.2};
DE Short=Sip-L {ECO:0000303|Ref.2};
GN Name=ADI1 {ECO:0000255|HAMAP-Rule:MF_03154};
GN Synonyms=MTCBP1 {ECO:0000255|HAMAP-Rule:MF_03154}; ORFNames=HMFT1638;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH MMP14,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Fibroblast;
RX PubMed=14718544; DOI=10.1074/jbc.m309957200;
RA Uekita T., Gotoh I., Kinoshita T., Itoh Y., Sato H., Shiomi T., Okada Y.,
RA Seiki M.;
RT "Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein-
RT 1 is a new member of the cupin superfamily. A possible multifunctional
RT protein acting as an invasion suppressor down-regulated in tumors.";
RL J. Biol. Chem. 279:12734-12743(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Fan Y.X., Yu L., Ding J.B., Hu P.R., Fu S.N., Zhao S.Y.;
RT "Cloning and expression of a new human cDNA homologous to O.sativa
RT submergence induced protein 2 (sip2) mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hepatoblastoma;
RX PubMed=15221005; DOI=10.1038/sj.onc.1207782;
RA Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S.,
RA Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S.,
RA Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.;
RT "Expression profiling and differential screening between hepatoblastomas
RT and the corresponding normal livers: identification of high expression of
RT the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas.";
RL Oncogene 23:5901-5911(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Ovarian carcinoma, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adipose tissue;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [9]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 2-30.
RC TISSUE=Leukemic T-cell;
RX PubMed=19892738; DOI=10.1073/pnas.0908958106;
RA Xu G., Shin S.B., Jaffrey S.R.;
RT "Global profiling of protease cleavage sites by chemoselective labeling of
RT protein N-termini.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 50-179, FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=11602742; DOI=10.1128/jvi.75.22.11017-11024.2001;
RA Yeh C.-T., Lai H.-Y., Chen T.-C., Chu C.-M., Liaw Y.-F.;
RT "Identification of a hepatic factor capable of supporting hepatitis C virus
RT replication in a nonpermissive cell line.";
RL J. Virol. 75:11017-11024(2001).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-94.
RX PubMed=15938715; DOI=10.1111/j.1365-2443.2005.00859.x;
RA Hirano W., Gotoh I., Uekita T., Seiki M.;
RT "Membrane-type 1 matrix metalloproteinase cytoplasmic tail binding protein-
RT 1 (MTCBP-1) acts as an eukaryotic aci-reductone dioxygenase (ARD) in the
RT methionine salvage pathway.";
RL Genes Cells 10:565-574(2005).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14] {ECO:0007744|PDB:4QGN}
RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) IN COMPLEX WITH IRON, AND COFACTOR.
RA Milaczewska A.M., Chruszcz M., Petkowski J.J., Niedzialkowska E., Minor W.,
RA Borowski T.;
RT "Human acireductone dioxygenase with iron ion and L-methionine in active
RT center.";
RL Submitted (MAY-2014) to the PDB data bank.
CC -!- FUNCTION: Catalyzes 2 different reactions between oxygen and the
CC acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene)
CC depending upon the metal bound in the active site (By similarity). Fe-
CC containing acireductone dioxygenase (Fe-ARD) produces formate and 2-
CC keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of
CC methionine in the methionine recycle pathway (PubMed:15938715). Ni-
CC containing acireductone dioxygenase (Ni-ARD) produces
CC methylthiopropionate, carbon monoxide and formate, and does not lie on
CC the methionine recycle pathway (By similarity). Also down-regulates
CC cell migration mediated by MMP14 (PubMed:14718544). Necessary for
CC hepatitis C virus replication in an otherwise non-permissive cell line
CC (PubMed:11602742). {ECO:0000255|HAMAP-Rule:MF_03154,
CC ECO:0000269|PubMed:11602742, ECO:0000269|PubMed:14718544,
CC ECO:0000269|PubMed:15938715}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4-
CC methylsulfanyl-2-oxobutanoate + formate + 2 H(+);
CC Xref=Rhea:RHEA:24504, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16723, ChEBI:CHEBI:49252;
CC EC=1.13.11.54; Evidence={ECO:0000269|PubMed:15938715};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 3-
CC (methylsulfanyl)propanoate + CO + formate + 2 H(+);
CC Xref=Rhea:RHEA:14161, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:17245, ChEBI:CHEBI:49016,
CC ChEBI:CHEBI:49252; EC=1.13.11.53; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03154};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|Ref.14};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000250|UniProtKB:Q99JT9};
CC Note=Binds either 1 Fe or Ni cation per monomer. Iron-binding promotes
CC an acireductone dioxygenase reaction producing 2-keto-4-
CC methylthiobutyrate, while nickel-binding promotes an acireductone
CC dioxygenase reaction producing 3-(methylsulfanyl)propanoate.
CC {ECO:0000250|UniProtKB:Q99JT9};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC step 5/6. {ECO:0000255|HAMAP-Rule:MF_03154}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with MMP14.
CC {ECO:0000255|HAMAP-Rule:MF_03154, ECO:0000269|PubMed:14718544}.
CC -!- INTERACTION:
CC Q9BV57; Q9UKG1: APPL1; NbExp=3; IntAct=EBI-992807, EBI-741243;
CC Q9BV57; P50281: MMP14; NbExp=4; IntAct=EBI-992807, EBI-992788;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000303|PubMed:14718544}. Nucleus
CC {ECO:0000303|PubMed:14718544}. Cell membrane
CC {ECO:0000303|PubMed:14718544}; Peripheral membrane protein
CC {ECO:0000303|PubMed:14718544}; Cytoplasmic side
CC {ECO:0000303|PubMed:14718544}. Note=Localizes to the plasma membrane
CC when complexed to MMP14. {ECO:0000303|PubMed:14718544}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BV57-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BV57-2; Sequence=VSP_015822;
CC -!- TISSUE SPECIFICITY: Detected in heart, colon, lung, stomach, brain,
CC spleen, liver, skeletal muscle and kidney.
CC {ECO:0000269|PubMed:11602742, ECO:0000269|PubMed:14718544}.
CC -!- SIMILARITY: Belongs to the acireductone dioxygenase (ARD) family.
CC {ECO:0000255|HAMAP-Rule:MF_03154}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL25800.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD38646.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD96187.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB158319; BAD10866.1; -; mRNA.
DR EMBL; AF087863; AAP97173.1; -; mRNA.
DR EMBL; AB073609; BAD38646.1; ALT_INIT; mRNA.
DR EMBL; AK001775; BAA91901.1; -; mRNA.
DR EMBL; AK127473; BAC86996.1; -; mRNA.
DR EMBL; AK222467; BAD96187.1; ALT_INIT; mRNA.
DR EMBL; AC142528; AAX82038.1; -; Genomic_DNA.
DR EMBL; AC114810; AAY24022.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX01064.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX01065.1; -; Genomic_DNA.
DR EMBL; BC001467; AAH01467.1; -; mRNA.
DR EMBL; AF403478; AAL25800.1; ALT_INIT; mRNA.
DR CCDS; CCDS1653.1; -. [Q9BV57-1]
DR CCDS; CCDS77380.1; -. [Q9BV57-2]
DR RefSeq; NP_001293006.1; NM_001306077.1. [Q9BV57-2]
DR RefSeq; NP_060739.2; NM_018269.3. [Q9BV57-1]
DR PDB; 4QGN; X-ray; 3.05 A; A=1-179.
DR PDB; 7JXG; NMR; -; A=1-179.
DR PDBsum; 4QGN; -.
DR PDBsum; 7JXG; -.
DR AlphaFoldDB; Q9BV57; -.
DR SMR; Q9BV57; -.
DR BioGRID; 120547; 36.
DR IntAct; Q9BV57; 3.
DR STRING; 9606.ENSP00000333666; -.
DR ChEMBL; CHEMBL3817720; -.
DR iPTMnet; Q9BV57; -.
DR MetOSite; Q9BV57; -.
DR PhosphoSitePlus; Q9BV57; -.
DR BioMuta; ADI1; -.
DR DMDM; 74733289; -.
DR EPD; Q9BV57; -.
DR jPOST; Q9BV57; -.
DR MassIVE; Q9BV57; -.
DR MaxQB; Q9BV57; -.
DR PaxDb; Q9BV57; -.
DR PeptideAtlas; Q9BV57; -.
DR PRIDE; Q9BV57; -.
DR ProteomicsDB; 79171; -. [Q9BV57-1]
DR ProteomicsDB; 79172; -. [Q9BV57-2]
DR TopDownProteomics; Q9BV57-1; -. [Q9BV57-1]
DR TopDownProteomics; Q9BV57-2; -. [Q9BV57-2]
DR Antibodypedia; 26318; 314 antibodies from 29 providers.
DR DNASU; 55256; -.
DR Ensembl; ENST00000327435.11; ENSP00000333666.3; ENSG00000182551.14. [Q9BV57-1]
DR Ensembl; ENST00000382093.5; ENSP00000371525.5; ENSG00000182551.14. [Q9BV57-2]
DR GeneID; 55256; -.
DR KEGG; hsa:55256; -.
DR MANE-Select; ENST00000327435.11; ENSP00000333666.3; NM_018269.4; NP_060739.2.
DR UCSC; uc002qxp.5; human. [Q9BV57-1]
DR CTD; 55256; -.
DR DisGeNET; 55256; -.
DR GeneCards; ADI1; -.
DR HGNC; HGNC:30576; ADI1.
DR HPA; ENSG00000182551; Tissue enhanced (liver).
DR MIM; 613400; gene.
DR neXtProt; NX_Q9BV57; -.
DR OpenTargets; ENSG00000182551; -.
DR PharmGKB; PA143485291; -.
DR VEuPathDB; HostDB:ENSG00000182551; -.
DR eggNOG; KOG2107; Eukaryota.
DR GeneTree; ENSGT00390000008195; -.
DR HOGENOM; CLU_090154_0_1_1; -.
DR InParanoid; Q9BV57; -.
DR OMA; RGQEDEW; -.
DR OrthoDB; 1166094at2759; -.
DR PhylomeDB; Q9BV57; -.
DR TreeFam; TF300231; -.
DR BRENDA; 1.13.11.53; 2681.
DR BRENDA; 1.13.11.54; 2681.
DR PathwayCommons; Q9BV57; -.
DR Reactome; R-HSA-1237112; Methionine salvage pathway.
DR SignaLink; Q9BV57; -.
DR UniPathway; UPA00904; UER00878.
DR BioGRID-ORCS; 55256; 9 hits in 1086 CRISPR screens.
DR ChiTaRS; ADI1; human.
DR GeneWiki; ADI1; -.
DR GenomeRNAi; 55256; -.
DR Pharos; Q9BV57; Tbio.
DR PRO; PR:Q9BV57; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9BV57; protein.
DR Bgee; ENSG00000182551; Expressed in right lobe of liver and 96 other tissues.
DR ExpressionAtlas; Q9BV57; baseline and differential.
DR Genevisible; Q9BV57; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0010308; F:acireductone dioxygenase (Ni2+-requiring) activity; IEA:RHEA.
DR GO; GO:0010309; F:acireductone dioxygenase [iron(II)-requiring] activity; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IDA:UniProtKB.
DR GO; GO:0006555; P:methionine metabolic process; IBA:GO_Central.
DR CDD; cd02232; cupin_ARD; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR HAMAP; MF_03154; Salvage_MtnD_euk; 1.
DR InterPro; IPR004313; ARD.
DR InterPro; IPR027496; ARD_euk.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR23418; PTHR23418; 1.
DR Pfam; PF03079; ARD; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Amino-acid biosynthesis; Cell membrane;
KW Cytoplasm; Dioxygenase; Direct protein sequencing; Iron; Membrane;
KW Metal-binding; Methionine biosynthesis; Nickel; Nucleus; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..179
FT /note="Acireductone dioxygenase"
FT /id="PRO_0000162942"
FT REGION 7..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 88
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /ligand_note="for iron-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000269|Ref.14"
FT BINDING 88
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="for nickel-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT BINDING 90
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /ligand_note="for iron-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000269|Ref.14"
FT BINDING 90
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="for nickel-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT BINDING 94
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /ligand_note="for iron-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000269|Ref.14"
FT BINDING 94
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="for nickel-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT BINDING 133
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /ligand_note="for iron-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000269|Ref.14"
FT BINDING 133
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_note="for nickel-dependent acireductone dioxygenase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT VAR_SEQ 1..40
FT /note="MVQAWYMDDAPGDPRQPHRPDPGRPVGLEQLRRLGVLYWK -> MSVKSSKL
FT MFLCHGSSRSLHSGSLTSCNTGVCCS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_015822"
FT MUTAGEN 94
FT /note="E->A: Loss of aci-reductone dioxygenase activity."
FT /evidence="ECO:0000269|PubMed:15938715"
FT CONFLICT 3
FT /note="Q -> L (in Ref. 4; BAA91901)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="R -> G (in Ref. 5; BAD96187)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="Q -> K (in Ref. 2; AAP97173)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:4QGN"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:7JXG"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:4QGN"
FT HELIX 28..32
FT /evidence="ECO:0007829|PDB:4QGN"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:4QGN"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:4QGN"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:4QGN"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:4QGN"
FT HELIX 50..58
FT /evidence="ECO:0007829|PDB:4QGN"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:4QGN"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:4QGN"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:7JXG"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:4QGN"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:4QGN"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:4QGN"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:7JXG"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:4QGN"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:4QGN"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:4QGN"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:7JXG"
FT STRAND 143..152
FT /evidence="ECO:0007829|PDB:4QGN"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:7JXG"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:4QGN"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:7JXG"
FT HELIX 166..176
FT /evidence="ECO:0007829|PDB:4QGN"
SQ SEQUENCE 179 AA; 21498 MW; 92E13B9718D44C27 CRC64;
MVQAWYMDDA PGDPRQPHRP DPGRPVGLEQ LRRLGVLYWK LDADKYENDP ELEKIRRERN
YSWMDIITIC KDKLPNYEEK IKMFYEEHLH LDDEIRYILD GSGYFDVRDK EDQWIRIFME
KGDMVTLPAG IYHRFTVDEK NYTKAMRLFV GEPVWTAYNR PADHFEARGQ YVKFLAQTA
