ID U2J640_9SPHI Unreviewed; 755 AA.
AC U2J640;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
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 ORFNames=M472_04925 {ECO:0000313|EMBL:ERJ58103.1};
OS Sphingobacterium paucimobilis HER1398.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1346330 {ECO:0000313|EMBL:ERJ58103.1, ECO:0000313|Proteomes:UP000016584};
RN [1] {ECO:0000313|EMBL:ERJ58103.1, ECO:0000313|Proteomes:UP000016584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HER1398 {ECO:0000313|EMBL:ERJ58103.1,
RC ECO:0000313|Proteomes:UP000016584};
RX PubMed=23929486;
RA White R.A.III., Suttle C.A.;
RT "The Draft Genome Sequence of Sphingomonas paucimobilis Strain HER1398
RT (Proteobacteria), Host to the Giant PAU Phage, Indicates That It Is a
RT Member of the Genus Sphingobacterium (Bacteroidetes).";
RL Genome Announc. 1:e00598-13(2013).
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:ERJ58103.1}.
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DR EMBL; ATDL01000018; ERJ58103.1; -; Genomic_DNA.
DR RefSeq; WP_021071583.1; NZ_ATDL01000018.1.
DR AlphaFoldDB; U2J640; -.
DR STRING; 1346330.M472_04925; -.
DR PATRIC; fig|1346330.5.peg.3445; -.
DR eggNOG; COG1048; Bacteria.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000016584; 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.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000016584}.
FT DOMAIN 35..477
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 558..685
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 755 AA; 81590 MW; 42B8A9E9C64DB73B CRC64;
MAFDIEMIKK VYSQYDERIK AARQIVNKPL TLSEKILYTH LWSGNATEAY ERGRSYVDFA
PDRVAMQDAT AQMALLQFMQ AGRAKAAVPS TVHCDHLIQA KEGADKDLAR AKSESSEVFN
FLSSVSNKYG IGFWKPGAGI IHQVVLENYA FPGGLMIGTD SHTVNAGGLG MVAIGVGGAD
ACDVMAGLPW ELKFPKLIGV KLTGKLTGWA ASKDVILKVA GILTVKGGTG AIVEYFGEGA
ESLSCSGKGT ICNMGAEIGA TTSTFGYDAA MERYLRATGR ADVADAANAI KEHLTADPEV
YANPELYFDQ IIEINLSELE PSLNGPFTPD LYTPASRMRE EAQKNGWPTK VEWGLIGSCT
NSSYEDLARA ASIARQAVEK GLVTKAEFGI NPGSEQVRYT ADRDGLLKTF EDLNATIFTN
ACGPCIGMWD RAGADKQEKN TIVHSFNRNF AKRADGNPNT YAFVTSPEMV AAIAISGDLG
FNPVTDTLTN KNGEQVKLDP PTGDELPTKG FDVEDPGYQA PAADGSSVVV DVSPTSDRLQ
LLEPFSPWEG TDLKGLKLLI KAKGKCTTDH ISMAGPWLKY RGHLDNISNN LLIGAVNYFN
DKTDNVQNQL TGEYGAVPAT QRAYKAAGIG SIVVGDENYG EGSSREHAAM EPRHLGVRAV
LVKSFARIHE TNLKKQGMLG LTFADKDDYD KIQENDTIDI LGLTEFAPNK PLTLVLHHVD
GSEDCISVNH TYNAQQIEWF KAGGALNIIR ANQAK
//
