HGD_ARATH
ID HGD_ARATH Reviewed; 461 AA.
AC Q9ZRA2; Q8L9I0; Q9LDB8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Homogentisate 1,2-dioxygenase;
DE EC=1.13.11.5;
DE AltName: Full=Homogentisate oxygenase;
DE AltName: Full=Homogentisic acid oxidase;
DE AltName: Full=Homogentisicase;
GN Name=HGO; OrderedLocusNames=At5g54080; ORFNames=MJP23.6;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Schmidt S.R., Werner E., Mueller C.R., Kress W.;
RT "Cloning and characterization of the homogentisate 1,2-dioxygenase gene in
RT A. thaliana and C. elegans.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Schmidt S.R.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=homogentisate + O2 = 4-maleylacetoacetate + H(+);
CC Xref=Rhea:RHEA:15449, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16169, ChEBI:CHEBI:17105; EC=1.13.11.5;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 4/6.
CC -!- SIMILARITY: Belongs to the homogentisate dioxygenase family.
CC {ECO:0000305}.
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DR EMBL; U80668; AAD00360.1; -; mRNA.
DR EMBL; AF130845; AAF36499.1; -; Genomic_DNA.
DR EMBL; AB018115; BAA97130.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96447.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96448.1; -; Genomic_DNA.
DR EMBL; AY140075; AAM98216.1; -; mRNA.
DR EMBL; BT010329; AAQ55280.1; -; mRNA.
DR EMBL; AY088421; AAM65958.1; -; mRNA.
DR RefSeq; NP_200219.1; NM_124787.4.
DR RefSeq; NP_851187.1; NM_180856.4.
DR AlphaFoldDB; Q9ZRA2; -.
DR SMR; Q9ZRA2; -.
DR STRING; 3702.AT5G54080.2; -.
DR iPTMnet; Q9ZRA2; -.
DR PaxDb; Q9ZRA2; -.
DR PRIDE; Q9ZRA2; -.
DR ProteomicsDB; 230235; -.
DR EnsemblPlants; AT5G54080.1; AT5G54080.1; AT5G54080.
DR EnsemblPlants; AT5G54080.2; AT5G54080.2; AT5G54080.
DR GeneID; 835494; -.
DR Gramene; AT5G54080.1; AT5G54080.1; AT5G54080.
DR Gramene; AT5G54080.2; AT5G54080.2; AT5G54080.
DR KEGG; ath:AT5G54080; -.
DR Araport; AT5G54080; -.
DR TAIR; locus:2166567; AT5G54080.
DR eggNOG; KOG1417; Eukaryota.
DR HOGENOM; CLU_027174_0_0_1; -.
DR InParanoid; Q9ZRA2; -.
DR OMA; FMFETRW; -.
DR OrthoDB; 795654at2759; -.
DR PhylomeDB; Q9ZRA2; -.
DR BioCyc; ARA:AT5G54080-MON; -.
DR BRENDA; 1.13.11.5; 399.
DR UniPathway; UPA00139; UER00339.
DR PRO; PR:Q9ZRA2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9ZRA2; baseline and differential.
DR Genevisible; Q9ZRA2; AT.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0004411; F:homogentisate 1,2-dioxygenase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1902000; P:homogentisate catabolic process; IDA:TAIR.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IBA:GO_Central.
DR GO; GO:0006572; P:tyrosine catabolic process; IGI:TAIR.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR005708; Homogentis_dOase.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR11056; PTHR11056; 1.
DR Pfam; PF04209; HgmA; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
DR TIGRFAMs; TIGR01015; hmgA; 1.
PE 2: Evidence at transcript level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Phenylalanine catabolism;
KW Reference proteome; Tyrosine catabolism.
FT CHAIN 1..461
FT /note="Homogentisate 1,2-dioxygenase"
FT /id="PRO_0000220244"
FT BINDING 341
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CONFLICT 7
FT /note="E -> K (in Ref. 6; AAM65958)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="V -> I (in Ref. 6; AAM65958)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="I -> T (in Ref. 6; AAM65958)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="T -> K (in Ref. 6; AAM65958)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="T -> S (in Ref. 6; AAM65958)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="S -> P (in Ref. 6; AAM65958)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="D -> E (in Ref. 1; AAD00360)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="S -> P (in Ref. 6; AAM65958)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 461 AA; 51455 MW; CD90DD9638014D31 CRC64;
MEEKKKELEE LKYQSGFGNH FSSEAIAGAL PLDQNSPLLC PYGLYAEQIS GTSFTSPRKL
NQRSWLYRVK PSVTHEPFKP RVPAHKKLVS EFDASNSRTN PTQLRWRPED IPDSEIDFVD
GLFTICGAGS SFLRHGFAIH MYVANTGMKD SAFCNADGDF LLVPQTGRLW IETECGRLLV
TPGEIAVIPQ GFRFSIDLPD GKSRGYVAEI YGAHFQLPDL GPIGANGLAA SRDFLAPTAW
FEDGLRPEYT IVQKFGGELF TAKQDFSPFN VVAWHGNYVP YKYDLKKFCP YNTVLLDHGD
PSINTVLTAP TDKPGVALLD FVIFPPRWLV AEHTFRPPYY HRNCMSEFMG LIYGAYEAKA
DGFLPGGASL HSCMTPHGPD TTTYEATIAR VNAMAPSKLT GTMAFMFESA LIPRVCHWAL
ESPFLDHDYY QCWIGLKSHF SRISLDKTNV ESTEKEPGAS E
