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   27-MAR-2024, entry version 190.
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; 43.
DR   IntAct; Q9BV57; 4.
DR   STRING; 9606.ENSP00000333666; -.
DR   ChEMBL; CHEMBL3817720; -.
DR   GlyGen; Q9BV57; 1 site, 1 O-linked glycan (1 site).
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; 9606-ENSP00000333666; -.
DR   PeptideAtlas; Q9BV57; -.
DR   ProteomicsDB; 79171; -. [Q9BV57-1]
DR   ProteomicsDB; 79172; -. [Q9BV57-2]
DR   Pumba; Q9BV57; -.
DR   TopDownProteomics; Q9BV57-1; -. [Q9BV57-1]
DR   TopDownProteomics; Q9BV57-2; -. [Q9BV57-2]
DR   Antibodypedia; 26318; 337 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   AGR; HGNC:30576; -.
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; MVRAWYM; -.
DR   OrthoDB; 130851at2759; -.
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; 12 hits in 1164 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 98 other cell types or tissues.
DR   ExpressionAtlas; Q9BV57; baseline and differential.
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:UniProtKB-UniRule.
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:0016151; F:nickel cation 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; Jelly Rolls; 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; ACIREDUCTONE DIOXYGENASE; 1.
DR   PANTHER; PTHR23418:SF0; ACIREDUCTONE DIOXYGENASE; 1.
DR   Pfam; PF03079; ARD; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
DR   Genevisible; Q9BV57; HS.
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
//