ID A0A093CSI8_9AVES Unreviewed; 774 AA.
AC A0A093CSI8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=N339_09336 {ECO:0000313|EMBL:KFV15252.1};
OS Pterocles gutturalis (yellow-throated sandgrouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Ciconiiformes; Pteroclidae; Pterocles.
OX NCBI_TaxID=240206 {ECO:0000313|EMBL:KFV15252.1, ECO:0000313|Proteomes:UP000053149};
RN [1] {ECO:0000313|EMBL:KFV15252.1, ECO:0000313|Proteomes:UP000053149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N339 {ECO:0000313|EMBL:KFV15252.1};
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; KL246715; KFV15252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093CSI8; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000053149; 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:UP000053149};
KW Transit peptide {ECO:0000256|RuleBase:RU362107}.
FT DOMAIN 58..494
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 575..702
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 522..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV15252.1"
FT NON_TER 774
FT /evidence="ECO:0000313|EMBL:KFV15252.1"
SQ SEQUENCE 774 AA; 84521 MW; 3F140EFF2082BCE9 CRC64;
QHALNSGIRR YHVAPVLCQR AKVAMSHFEP NEYINYEKLE KNINIVRKRL DRPLTLSEKI
VYGHLDDPAK QEIERGKTYL RLRPDRVAMQ DATAQMAMLQ FISSGLPKVA VPSTIHCDHL
IEAQSGGEKD LQRAKDINQE VYNFLATAGA KYGVGFWKPG SGIIHQIILE NYSYPGVMLI
GTDSHTPNGG GLGGICIGVG GADAVDVMAG IPWELKCPKV IGVKLTGKLS GWSSPKDVIL
KVAGILTVKG GTGAIIEYHG PGVDSISCTG MATICNMGAE IGATTSIFPY NARMKKYLGK
TGRADIAALA DEFQQHLVPD SGCQYDQVIE INLSELKPHI NGPFTPDLAH PVSDIGAVAE
KEGWPVDIRV GLIGSCTNSS YEDMGRSAAV AKQALAHGLK CKSKFTITPG SEQIRATIER
DGYAQILRDV GGLVLANACG PCIGQWDRKD IKKGEKNTIV TSYNRNFTGR NDANPETHAF
VTSPEIVTAL SIAGTLKFNP ETDYLTGTDG KKFKLEAPDA DELPKLEFDP GQDTYQYPPK
DGSGQHVDVS PTSQRLQLLE PFDKWDGKDL EDMLILIKVK GKCTTDHISA AGPWLKFRGH
LDNISNNLLI GAINIENGKA NSVRNALTQE FGPVPDTARY YKKMGVKWAV IGDENYGEGS
SREHAALEPR HLGGRVIITK SFARIHETNL KKQGLLPLTF ADPADYNKIH PVDKLSIVGL
KDFTPGKPLK CIIKHPNGSQ ETIMLNHTFN ESQIEWFQAG SALNRMKELQ QKSS
//
