ID A0A105TS85_9FLAO Unreviewed; 754 AA.
AC A0A105TS85;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Aconitate hydratase A {ECO:0000256|ARBA:ARBA00019378};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
DE AltName: Full=Citrate hydro-lyase {ECO:0000256|ARBA:ARBA00029682};
DE AltName: Full=Iron-responsive protein-like {ECO:0000256|ARBA:ARBA00031977};
DE AltName: Full=RNA-binding protein {ECO:0000256|ARBA:ARBA00031081};
GN Name=acn {ECO:0000313|EMBL:KVV14228.1};
GN ORFNames=AP058_02114 {ECO:0000313|EMBL:KVV14228.1};
OS Flavobacterium sp. TAB 87.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1729581 {ECO:0000313|EMBL:KVV14228.1, ECO:0000313|Proteomes:UP000059935};
RN [1] {ECO:0000313|EMBL:KVV14228.1, ECO:0000313|Proteomes:UP000059935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAB87 {ECO:0000313|EMBL:KVV14228.1,
RC ECO:0000313|Proteomes:UP000059935};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00023501};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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 -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185}.
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:KVV14228.1}.
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DR EMBL; LLWK01000037; KVV14228.1; -; Genomic_DNA.
DR RefSeq; WP_066311118.1; NZ_LLWK01000037.1.
DR AlphaFoldDB; A0A105TS85; -.
DR STRING; 1729581.AP058_02114; -.
DR PATRIC; fig|1729581.3.peg.2186; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000059935; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000313|EMBL:KVV14228.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000059935}.
FT DOMAIN 52..477
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 558..686
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 754 AA; 81331 MW; 1999DC8ECD983066 CRC64;
MAFDIEMIKK VYENMPSRVD KAREIVGRPL TLTEKTLYNH LWDGMPTQAF GRGVEYVDFA
PDRVACQDAT AQMALLQFMH AGKPKVAVPT TVHCDHLIQA KVGAEADLKR AKSQSNEVFD
FLSSVSNKYG IGFWKPGAGI IHQVVLENYA FPGGMMIGTD SHTVNAGGLG MIAIGVGGAD
AVDVMSGMAW ELKFPKLIGV KLTGKLSGWT APKDVILKVA GILTVKGGTG AIVEYFGEGA
TAMSCTGKGT ICNMGAEIGA TTSTFGYDDS MGRYLRATNR ADVADAADKI APYLTGDPEV
YAEPEKYFDQ VIEINLSELE PHLNGPFTPD LATPISKMKE AAIKNNWPLQ IQVGLIGSCT
NSSYEDISRA ASLAKQVADK KLKTKAKFAI NPGSETIRYT IERDGFIDTF EKIGATVFAN
ACGPCIGMWD REGAEKEERN TIVHSFNRNF SKRADGNPNT LAFVGSPELV TALAIAGDLG
FNPLTDTLIN EDGEEVRLEE PTGDELPPNG FDVEDPGFQA PAHDGSNVVV SVNPESERLQ
LLAPFKPWDG QNIVGAKLLI KAFGKCTTDH ISMAGPWLRF RGHLDNISNN MLIGAINAFN
QKTNSVKNQL TGVYDAVPAV ARAYKAAGVP SIVVGDHNYG EGSSREHAAM EPRFLGVEAV
LVKSFARIHE TNLKKQGLLG LTFANEADYD KIQENDTINF LDLVDFAPGK PLSIEFVHEN
GSKDVIVANH TYNEGQIGWF IAGSALNLIA ADNA
//
