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
//