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Database: UniProt
Entry: A0A0F9WZT1_TRIHA
LinkDB: A0A0F9WZT1_TRIHA
Original site: A0A0F9WZT1_TRIHA 
ID   A0A0F9WZT1_TRIHA        Unreviewed;      1898 AA.
AC   A0A0F9WZT1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Homoaconitase, mitochondrial {ECO:0000256|ARBA:ARBA00021560, ECO:0000256|RuleBase:RU362038};
DE            EC=4.2.1.36 {ECO:0000256|RuleBase:RU362038};
DE   AltName: Full=Homoaconitate hydratase {ECO:0000256|RuleBase:RU362038};
GN   ORFNames=THAR02_09943 {ECO:0000313|EMBL:KKO97954.1};
OS   Trichoderma harzianum (Hypocrea lixii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=5544 {ECO:0000313|EMBL:KKO97954.1, ECO:0000313|Proteomes:UP000034112};
RN   [1] {ECO:0000313|Proteomes:UP000034112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6776 {ECO:0000313|Proteomes:UP000034112};
RX   PubMed=26067977; DOI=10.1128/genomeA.00647-15;
RA   Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA   Pe M.E., Sarrocco S., Vannacci G.;
RT   "Draft whole-genome sequence of the biocontrol agent Trichoderma harzianum
RT   T6776.";
RL   Genome Announc. 3:E0064715-E0064715(2015).
CC   -!- FUNCTION: Catalyzes the reversible hydration of cis-homoaconitate to
CC       (2R,3S)-homoisocitrate, a step in the alpha-aminoadipate pathway for
CC       lysine biosynthesis. {ECO:0000256|ARBA:ARBA00003422,
CC       ECO:0000256|RuleBase:RU362038}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-homoisocitrate = cis-homoaconitate + H2O;
CC         Xref=Rhea:RHEA:15485, ChEBI:CHEBI:15377, ChEBI:CHEBI:15404,
CC         ChEBI:CHEBI:58174; EC=4.2.1.36;
CC         Evidence={ECO:0000256|ARBA:ARBA00029338,
CC         ECO:0000256|RuleBase:RU362038};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|RuleBase:RU362038};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.
CC       {ECO:0000256|RuleBase:RU362038};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC       pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 3/5.
CC       {ECO:0000256|ARBA:ARBA00005106, ECO:0000256|RuleBase:RU362038}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC       ECO:0000256|RuleBase:RU362038}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC       {ECO:0000256|ARBA:ARBA00007705}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000256|RuleBase:RU362038}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKO97954.1}.
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DR   EMBL; JOKZ01000482; KKO97954.1; -; Genomic_DNA.
DR   OrthoDB; 5403095at2759; -.
DR   UniPathway; UPA00033; UER01027.
DR   Proteomes; UP000034112; Unassembled WGS sequence.
DR   GO; GO:0005760; C:gamma DNA polymerase complex; IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro.
DR   GO; GO:0004409; F:homoaconitate hydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniRule.
DR   GO; GO:0006264; P:mitochondrial DNA replication; IEA:InterPro.
DR   CDD; cd08641; DNA_pol_gammaA; 1.
DR   CDD; cd01674; Homoaconitase_Swivel; 1.
DR   Gene3D; 3.30.420.390; -; 2.
DR   Gene3D; 3.30.70.370; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR   Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR   InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR   InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR   InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR   InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR   InterPro; IPR002297; DNA-dir_DNA_pol_A_mt.
DR   InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR041336; DNApol_Exo.
DR   InterPro; IPR004418; Homoaconitase_mito.
DR   InterPro; IPR039386; Homoaconitase_swivel.
DR   InterPro; IPR047580; POLG_palm_dom.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   NCBIfam; TIGR00139; h_aconitase; 1.
DR   PANTHER; PTHR10267; DNA POLYMERASE SUBUNIT GAMMA-1; 1.
DR   PANTHER; PTHR10267:SF0; DNA POLYMERASE SUBUNIT GAMMA-1; 1.
DR   Pfam; PF00330; Aconitase; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   Pfam; PF18136; DNApol_Exo; 1.
DR   PRINTS; PR00867; DNAPOLG.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
DR   PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU362038};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362038};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU362038};
KW   Lyase {ECO:0000256|RuleBase:RU362038};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154,
KW   ECO:0000256|RuleBase:RU362038}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362038};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW   ECO:0000256|RuleBase:RU362038};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034112};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW   ECO:0000256|RuleBase:RU362038}.
FT   DOMAIN          697..927
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
FT   REGION          1066..1109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1066..1094
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1898 AA;  211243 MW;  39B983E4ACDB80C0 CRC64;
     MRALYSAAGK LQRAPVASFV RLARLRGRRI AWEAQSRWLA DVVQRDEAKE TKSLALSSSS
     RYNEVGVQQL SDHIFPQVFP GGSKPPPEEL VRLSRDHLKR HDLYGKNTDT SEPVAFDLPE
     LKGKTLDEHF HKLGIDCAEP YLRLAKEFAC ANVPLKPKQW VHQSGWTKYH SDGTPPESVE
     SPDEEMLCFD TEVMYKNHHF AVMACAVSPT AWYSWLSPWL LGETDNERQL IPMGDPTKDR
     IIVGHNVGYD RARILEEYDL KQTRTGFLDT MSLHVAVNGM CSRQRPTWQR FKKNREMRER
     VASQDPDHGM VELLSNPSIH EEEELWVERS SVNSLRDVAK FHLNVTIDKS KRDDFAETDR
     EVILKQLDQL LEYCAADVST THRVYQIVLP SFLNVCPHPV SFAALRHLSS VILPVNETWE
     QYIANADALY NNLLESVQKR LEDLAEKAKE LKDRPEIWEK DPWMMQLDWT KSEERLVKSK
     DNPGKKVPDK RQKKAGEPKW YRDLFANKDA PINLTVRSRI APLLLKLAWD GHPLFWSNKY
     GWVFRVNPTD VSGYIAKKMP ECVFDDSDPA LRADWGHSYF KLPHKDGPTA RCSNPMAKGY
     LNYFENGTLS SEYEYAKEAL EMNASCSYWI SARDRIRSQM VVYENDILAT GEGKAMEAGE
     KRQGFILPQV IPMGTITRRA VEKTWLTASN AKKNRVGSEL KSMVKAPDGY CFVGADVDSE
     ELWIASLMGD ATFKIHGGNA IGFMTLEGTK AAGTDLHSRT AAILGITRND AKVFNYGRIY
     GAGLNFAATL LRQFNPALSE SETMTIAQRL YANTKGTKTI RRVINQHKFW RGGTESFVFN
     KLEEFAEQDW ARTPVLGAGI TQALMSRFVS KGGYLPSRIN WAIQSSGVDY LHLLIVSMDY
     LIRRFNLDAR LAITVHDEIR YLVKNEDKYR AALALQVANI WTRAMFAQQV GINDLPQSCA
     FFSAVDIDHV LRKEVNMDCV TPSHKTPIPH GESLDIQTLL GKGAEAMLDP SIVPDPKFAP
     KLDDIAYTPR TPIMQTLQES GQNNISFIKA QIANDDQELQ DIVNNLRKAT TPKSTTPRST
     TSRSTTSRST TPKYKAQMPR APPPEDVPRH NATDAEIAEL WCTWRRAIAV NASALAARQA
     RASITRSRLL LESVPQFRTY TLSSPRRQQA FQSQIDSTPR SSVLQSSLGA APANPQTLTE
     KIVQLHADGL LEGKKVRAGD YITLRPHKSM THDNSWPVIT KYMEMGATSV KDNRQVVMTL
     DHDVQNTSEQ NLRKYRLIEE FANTHGIDFY PAKHGIGHQI MIEEGYAWPG TVSVASDSHS
     NMYGGVGCLG TAIVRSDAAS VLATSTVFWQ IPPTVKITFT GVLPPGVTGK DTIIALCGLL
     NKDDVLNMCV EFTGSEQTLA SIPISERLTI ANMTTEWGAL SGLFPVDDKL ISWYRARATL
     AAMSNSPTKD RINHERIDKL LENPMVADPG AKYAKEFYFN LSTLSPFVAG PNSVKVANPV
     KNLEAQDIAV DKAYLLSCTN GRSEDFAAAA RVFREAGKDG KPAKVHPRVK FYLAPASVAE
     QKMAEDAGDW QILEQSGAQL LPAGCGPCIG LGTGLLEEGE VGISASNRNY KGRMGSPKAL
     CYLASPEVVA ASAIQGKIAS PGWYQKPEGV EKVVFGEGSG DFAADKARAV GDAFDKILGE
     MESLIGAAEG AAEESASPAA TEEETLTTVV PGFPEKIEGE IVFCDNDNIN TDGIYPGKYT
     YQDGLTTEQM AKVCMENYDT EFGNIIRPND VLVTGFNFGC GSSREQAATS ILAKQIPLVV
     AGSFGNIFSR NSINNALLGI EIPKLIERLR EAYKNDAEKP LTRRTGWKLL WDVRRSKVTI
     TEQDGSSWEQ KVGEMPPSVQ EIVAKGGVVK WVQSKMQA
//
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