ID A0A093HDP5_GAVST Unreviewed; 773 AA.
AC A0A093HDP5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Aconitate hydratase, mitochondrial {ECO:0000256|ARBA:ARBA00015940, ECO:0000256|RuleBase:RU362107};
DE Short=Aconitase {ECO:0000256|RuleBase:RU362107};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926, ECO:0000256|RuleBase:RU362107};
DE Flags: Fragment;
GN ORFNames=N328_08451 {ECO:0000313|EMBL:KFV52753.1};
OS Gavia stellata (Red-throated diver) (Colymbus stellatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gaviiformes; Gaviidae; Gavia.
OX NCBI_TaxID=37040 {ECO:0000313|EMBL:KFV52753.1, ECO:0000313|Proteomes:UP000054313};
RN [1] {ECO:0000313|EMBL:KFV52753.1, ECO:0000313|Proteomes:UP000054313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N328 {ECO:0000313|EMBL:KFV52753.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate. {ECO:0000256|ARBA:ARBA00003113}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336,
CC ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3;
CC Evidence={ECO:0000256|RuleBase:RU362107};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|RuleBase:RU362107};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000256|RuleBase:RU362107};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC ECO:0000256|RuleBase:RU362107}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU362107}.
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DR EMBL; KK624575; KFV52753.1; -; Genomic_DNA.
DR RefSeq; XP_009809234.1; XM_009810932.1.
DR AlphaFoldDB; A0A093HDP5; -.
DR KEGG; gste:104256477; -.
DR CTD; 50; -.
DR OrthoDB; 3266779at2759; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000054313; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd01578; AcnA_Mitochon_Swivel; 1.
DR CDD; cd01584; AcnA_Mitochondrial; 1.
DR Gene3D; 3.40.1060.10; Aconitase, Domain 2; 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; IPR015932; Aconitase_dom2.
DR InterPro; IPR006248; Aconitase_mito-like.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR01340; aconitase_mito; 1.
DR PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR PANTHER; PTHR43160:SF3; ACONITATE HYDRATASE, MITOCHONDRIAL; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362107};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU362107};
KW Lyase {ECO:0000256|RuleBase:RU362107};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362107};
KW Mitochondrion {ECO:0000256|RuleBase:RU362107};
KW Reference proteome {ECO:0000313|Proteomes:UP000054313};
KW Transit peptide {ECO:0000256|RuleBase:RU362107}.
FT DOMAIN 57..493
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 574..701
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 521..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV52753.1"
FT NON_TER 773
FT /evidence="ECO:0000313|EMBL:KFV52753.1"
SQ SEQUENCE 773 AA; 84331 MW; D8D3BD9525C55E48 CRC64;
HVLNSGIRHY HVAPVLCQRA KVAMSHFEPN EHINYEKLEK NINIVRKRLD RPLTLSEKIV
YGHLDDPAKQ EIERGKTYLR LRPDRVAMQD ATAQMAMLQF ISSGLPKVAV PSTIHCDHLI
EAQSGGEKDL RRAKDINQEV YNFLATAGAK YGVGFWKPGS GIIHQIILEN YSYPGVMLIG
TDSHTPNGGG LGGICIGVGG ADAVDVMAGI PWELKCPKVI GVKLTGKLSG WSSPKDVILK
VAGILTVKGG TGAIIEYHGP GVDSISCTGM ATICNMGAEI GATTSVFPYN ARMKKYLGKT
GRADIAALAD EFQQHLVPDS GCQYDQVIEI NLSELKPHIN GPFTPDLAHP VSDIGAVAEK
EGWPVDIRVG LIGSCTNSSY EDMGRSAAVA KQALEHGLKC KSKFTITPGS EQIRATIERD
GYAQILRDVG GLVLANACGP CIGQWDRKDI KKGEKNTIVT SYNRNFTGRN DANPETHAFV
TSPEIVTALS IAGTLKFNPE TDYLTGADGK KFKLEAPDAD ELPKLEFDPG QDTYQYPPKD
GSGQHVDVSP TSQRLQLLEP FDKWDGKDLE DMLILIKVKG KCTTDHISAA GPWLKFRGHL
DNISNNLLIG AINIENGKAN SVRNALTQEF GPVPDTARYY KKMGVKWAVI GDENYGEGSS
REHAALEPRH LGGRVIITKS FARIHETNLK KQGLLPLTFA DPADYNKIHP VDKLSIVGLA
DFAPGKPLKC IIKHPNGSQE TIMLNHTFNE SQIEWFQAGS ALNRMKELQQ KSS
//
