ID A0A238ZL13_9BACT Unreviewed; 764 AA.
AC A0A238ZL13;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=SAMN06269173_108138 {ECO:0000313|EMBL:SNR84126.1};
OS Hymenobacter mucosus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1411120 {ECO:0000313|EMBL:SNR84126.1, ECO:0000313|Proteomes:UP000198310};
RN [1] {ECO:0000313|EMBL:SNR84126.1, ECO:0000313|Proteomes:UP000198310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28041 {ECO:0000313|EMBL:SNR84126.1,
RC ECO:0000313|Proteomes:UP000198310};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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}.
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DR EMBL; FZNS01000008; SNR84126.1; -; Genomic_DNA.
DR RefSeq; WP_045687771.1; NZ_FZNS01000008.1.
DR AlphaFoldDB; A0A238ZL13; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000198310; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 34..477
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 558..687
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 764 AA; 82240 MW; 265F5E7BA8E50D8F CRC64;
MAFDLEMIKA VYDGMGSRIE AARTAVGRPL TLTEKILYAH LYGGSVSQAY ERGVSYVDFA
PDRVAMQDAT AQMALLQFMQ AGKPQVAVPS TVHCDHLIQA KEGADEDLAI ANSENREVYD
FLASVSNKYG IGFWKPGAGI IHQVVLENYA FPGGMMIGTD SHTPNAGGLG MIAIGVGGAD
AVDVMAGMAW ELKFPKVIGV KLTGKLSGWT APKDVILKVA GILTVKGGTG AIVEYFGEGA
ESMSCTGKAT ICNMGAEIGA TTSVFSYDDK MSDYLRGTER AEVAAMADGV RQHLRADEEV
YANPAAFYDQ LIEINLSELE PHVNGPFTPD AAWPISQFAS AVREHGWPEK LEVGLIGSCT
NSSYEDITRA ASVAEQAVQK GLTVSAEFTV TPGSELVRYT VERDGLLDTF AQMGGVVLAN
ACGPCIGQWA RHTDDPKRRN SIITSFNRNF AKRNDGNPNT HAFVASPEIV TAFAIAGDLT
FNPLVDTLTT KDGQQVKLDE PHGLEMPPQG YAVEDAGFQA PAADGTGVQV IVDPTSDRLE
LLDPFKPWEG TDLKGLRLLI KAQGKCTTDH ISMAGPWLKY RGHLDNISNN MLIGAINAFN
GEANSVKDGM TQGTPYSAVP QVARNYKAQG IGSIVVGDEN YGEGSSREHA AMEPRHLGVR
AILVKSFARI HETNLKKQGM LALTFANKAD YDLIEEDDTF DILGLTEFAP GKPLQIRLHH
ADGDTDLITV NHTYNQGQIE WFKAGSALNL IRLKESGEAQ LSQK
//